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8QXXHCMV DNA polymerase processivity factor UL44 phosphorylated NLS 410-433 bound to mouse importin alpha 22023 · 1.9 Å

Proteins: DNA polymerase processivity factor (Human betaherpesvirus 5); Importin subunit alpha-1 (Mus musculus)
Resolution: 1.9 Å · R_work 0.175, R_free 0.204
Space group: P 21 21 21
Cell: a = 78.9, b = 89.8, c = 97.6 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 58.1 kDa · 534 residues in 2 chains · 3,777 atoms
Data: Australian Synchrotron, MX2 · 0.95372 Å · DECTRIS EIGER X 16M
Timeline: Collected Mar 2019, deposited Oct 2023, released Nov 2023 · 4.6 years from beam to release
Validation: Clashscore 5.8 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Structural determinants of phosphorylation-dependent nuclear transport of HCMV DNA polymerase processivity factor UL44. (Febs Lett., 2024) · cited 9 times (OpenAlex)
What came after: 31 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (P16790)PDBe-KB (P52293)UniProt P16790 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

8QXWHCMV DNA polymerase processivity factor UL44 unphosphorylated NLS 410-433 bound to mouse importin alpha 22023 · 2 Å

Proteins: DNA polymerase processivity factor (Human betaherpesvirus 5); Importin subunit alpha-1 (Mus musculus)
Resolution: 2 Å · R_work 0.191, R_free 0.221
Space group: P 21 21 21
Cell: a = 78.9, b = 90.1, c = 96.1 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 58.0 kDa · 534 residues in 2 chains · 3,510 atoms
Data: Australian Synchrotron, MX2 · 0.95372 Å · DECTRIS EIGER X 16M
Timeline: Collected Mar 2019, deposited Oct 2023, released Nov 2023 · 4.6 years from beam to release
Validation: Clashscore 5.8 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Structural determinants of phosphorylation-dependent nuclear transport of HCMV DNA polymerase processivity factor UL44. (Febs Lett., 2024) · cited 9 times (OpenAlex)
What came after: 31 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (P16790)PDBe-KB (P52293)UniProt P16790 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RG6Importin alpha2 in complex with ORF4B Bat coronavirus HKU52021 · 2.1 Å

Proteins: Non-structural protein ORF4b (Bat coronavirus HKU5); Importin subunit alpha-1 (Mus musculus)
Resolution: 2.1 Å · R_work 0.205, R_free 0.223
Space group: P 21 21 21
Cell: a = 78.7, b = 90.3, c = 100.0 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 60.7 kDa · 550 residues in 3 chains · 3,549 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Mar 2021, deposited July 2021, released Aug 2021 · 5 months from beam to release
Validation: Clashscore 1.3 · Ramachandran outliers 0.0% · rotamer outliers 0.5%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 48 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (A3EXD3)PDBe-KB (P52293)UniProt A3EXD3 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RG5Importin alpha3 in complex with p50 NLS2021 · 2.15 Å

Proteins: Isoform 3 of Nuclear factor NF-kappa-B p105 subunit (Homo sapiens); Importin subunit alpha-3 (Homo sapiens)
Resolution: 2.15 Å · R_work 0.226, R_free 0.262
Space group: P 1 21 1
Cell: a = 47.8, b = 59.2, c = 86.2 Å; α = 90.0, β = 96.3, γ = 90.0°
Size: 55.3 kDa · 499 residues in 2 chains · 3,357 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Sept 2017, deposited July 2021, released Aug 2021 · 3.9 years from beam to release
Validation: Clashscore 1.4 · Ramachandran outliers 0.2% · rotamer outliers 0.5%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 5 later structures of Importin subunit alpha-3 in the PDB

PDBe PDBe-KB (P19838)PDBe-KB (O00629)UniProt P19838 UniProt O00629 AlphaFold O00629 PDB-REDO Validation report RCSB PDB

7RG4Importin alpha2 in complex with p50 NLS2021 · 2.6 Å

Proteins: Importin subunit alpha-1 (Mus musculus); Isoform 3 of Nuclear factor NF-kappa-B p105 subunit (Homo sapiens)
Resolution: 2.6 Å · R_work 0.217, R_free 0.243
Space group: P 21 21 21
Cell: a = 78.0, b = 89.7, c = 97.2 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 60.2 kDa · 550 residues in 2 chains · 3,318 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Nov 2017, deposited July 2021, released Aug 2021 · 3.8 years from beam to release
Validation: Clashscore 1.9 · Ramachandran outliers 0.0% · rotamer outliers 0.6%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 48 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (P52293)PDBe-KB (P19838)UniProt P52293 UniProt P19838 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RG3Importin alpha2 in complex with MERS ORF4B R37A mutant2021 · 2 Å

Proteins: ORF4b (Middle East respiratory syndrome-related coronavirus); Importin subunit alpha-1 (Mus musculus)
Resolution: 2 Å · R_work 0.177, R_free 0.194
Space group: P 21 21 21
Cell: a = 78.7, b = 90.0, c = 100.5 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 60.5 kDa · 552 residues in 3 chains · 3,669 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Dec 2020, deposited July 2021, released Aug 2021 · 9 months from beam to release
Validation: Clashscore 1.2 · Ramachandran outliers 0.0% · rotamer outliers 1.9%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 48 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (K9N643)PDBe-KB (P52293)UniProt K9N643 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RG2Importin alpha2 in complex with MERS ORF4B R33A mutant2021 · 2 Å

Proteins: ORF4b (Middle East respiratory syndrome-related coronavirus); Importin subunit alpha-1 (Mus musculus)
Resolution: 2 Å · R_work 0.199, R_free 0.216
Space group: P 21 21 21
Cell: a = 78.9, b = 89.9, c = 100.5 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 57.9 kDa · 531 residues in 2 chains · 3,606 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Dec 2020, deposited July 2021, released Aug 2021 · 9 months from beam to release
Validation: Clashscore 1.5 · Ramachandran outliers 0.0% · rotamer outliers 1.4%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 48 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (K9N643)PDBe-KB (P52293)UniProt K9N643 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RG1Importin alpha2 in complex with MERS ORF4B H26A mutant2021 · 1.85 Å

Proteins: ORF4b (Middle East respiratory syndrome-related coronavirus); Importin subunit alpha-1 (Mus musculus)
Resolution: 1.85 Å · R_work 0.200, R_free 0.211
Space group: P 21 21 21
Cell: a = 79.0, b = 89.7, c = 100.6 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 57.9 kDa · 531 residues in 2 chains · 3,697 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER2 X 16M
Timeline: Collected Dec 2020, deposited July 2021, released July 2021 · 8 months from beam to release
Validation: Clashscore 1.0 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMPα and block innate immunity. (Nat Commun, 2022)
What came after: 52 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (K9N643)PDBe-KB (P52293)UniProt K9N643 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RG0Importin alpha2 in complex with MERS ORF4B R24A mutant2021 · 2 Å

Proteins: ORF4b (Middle East respiratory syndrome-related coronavirus); Importin subunit alpha-1 (Mus musculus)
Resolution: 2 Å · R_work 0.195, R_free 0.213
Space group: P 21 21 21
Cell: a = 78.7, b = 89.6, c = 99.8 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 57.9 kDa · 531 residues in 2 chains · 3,531 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER2 X 16M
Timeline: Collected Dec 2020, deposited July 2021, released July 2021 · 8 months from beam to release
Validation: Clashscore 0.8 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 52 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (K9N643)PDBe-KB (P52293)UniProt K9N643 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RFZImportin alpha 2 in complex with MERS ORF4B NLS peptide2021 · 1.95 Å

Proteins: ORF4b (Middle East respiratory syndrome-related coronavirus); Importin subunit alpha-1 (Mus musculus)
Resolution: 1.95 Å · R_work 0.188, R_free 0.211
Space group: P 21 21 21
Cell: a = 78.5, b = 89.5, c = 100.1 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 58.0 kDa · 531 residues in 2 chains · 3,574 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Dec 2020, deposited July 2021, released July 2021 · 8 months from beam to release
Validation: Clashscore 1.3 · Ramachandran outliers 0.0% · rotamer outliers 0.5%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 52 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (K9N643)PDBe-KB (P52293)UniProt K9N643 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

7RFYImportin alpha3 in complex with MERS ORF4B2021 · 2.5 Å

Proteins: ORF4b (Middle East respiratory syndrome-related coronavirus); Importin subunit alpha-3 (Homo sapiens)
Resolution: 2.5 Å · R_work 0.249, R_free 0.267
Space group: P 1 21 1
Cell: a = 48.2, b = 59.7, c = 82.6 Å; α = 90.0, β = 98.9, γ = 90.0°
Size: 53.0 kDa · 480 residues in 2 chains · 3,143 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Aug 2020, deposited July 2021, released July 2021 · 12 months from beam to release
Validation: Clashscore 6.0 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 6 later structures of Importin subunit alpha-3 in the PDB

PDBe PDBe-KB (K9N643)PDBe-KB (O00629)UniProt K9N643 UniProt O00629 AlphaFold O00629 PDB-REDO Validation report RCSB PDB

7RFXImportin alpha2 in complex with MERS ORF4B2021 · 2.1 Å

Proteins: ORF4b (Middle East respiratory syndrome-related coronavirus); Importin subunit alpha-1 (Mus musculus)
Resolution: 2.1 Å · R_work 0.197, R_free 0.208
Space group: P 21 21 21
Cell: a = 79.3, b = 89.7, c = 99.4 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 58.0 kDa · 531 residues in 2 chains · 3,630 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 210r
Timeline: Collected Aug 2020, deposited July 2021, released July 2021 · 12 months from beam to release
Validation: Clashscore 1.0 · Ramachandran outliers 0.0% · rotamer outliers 0.5%
Paper: MERS-CoV ORF4b employs an unusual binding mechanism to target IMP alpha and block innate immunity. (Nat Commun, 2022) · cited 29 times (OpenAlex)
What came after: 52 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (K9N643)PDBe-KB (P52293)UniProt K9N643 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

6WX9SOX2 bound to Importin-alpha 52020 · 2.8 Å

Proteins: Transcription factor SOX-2 (Homo sapiens); Importin subunit alpha-5 (Homo sapiens)
Resolution: 2.8 Å · R_work 0.206, R_free 0.251
Space group: C 1 2 1
Cell: a = 160.5, b = 61.4, c = 69.1 Å; α = 90.0, β = 95.5, γ = 90.0°
Size: 62.8 kDa · 557 residues in 2 chains · 3,462 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Feb 2019, deposited May 2020, released Oct 2020 · 20 months from beam to release
Validation: Clashscore 10.7 · Ramachandran outliers 0.0% · rotamer outliers 0.8%
Paper: Structural basis for nuclear import selectivity of pioneer transcription factor SOX2. (Nat Commun, 2021) · cited 40 times (OpenAlex)
What came after: 0 later structures of Importin subunit alpha-5 in the PDB

PDBe PDBe-KB (P48431)PDBe-KB (P52294)UniProt P48431 UniProt P52294 AlphaFold P52294 PDB-REDO Validation report RCSB PDB

6WX8SOX2 bound to Importin-alpha 32020 · 2.3 Å

Proteins: Transcription factor SOX-2 (Homo sapiens); Importin subunit alpha-3 (Homo sapiens)
Resolution: 2.3 Å · R_work 0.220, R_free 0.245
Space group: C 1 2 1
Cell: a = 148.6, b = 119.0, c = 94.9 Å; α = 90.0, β = 128.8, γ = 90.0°
Size: 123.2 kDa · 1,098 residues in 4 chains · 8,113 atoms
Ligands: SO4
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Sept 2018, deposited May 2020, released Oct 2020 · 2.1 years from beam to release
Validation: Clashscore 3.1 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: Structural basis for nuclear import selectivity of pioneer transcription factor SOX2. (Nat Commun, 2021) · cited 40 times (OpenAlex)
What came after: 7 later structures of Importin subunit alpha-3 in the PDB

PDBe PDBe-KB (P48431)PDBe-KB (O00629)UniProt P48431 UniProt O00629 AlphaFold O00629 PDB-REDO Validation report RCSB PDB

6WX7SOX2 bound to Importin-alpha 22020 · 2.7 Å

Proteins: Transcription factor SOX-2 (Homo sapiens); Importin subunit alpha-1 (Mus musculus)
Resolution: 2.7 Å · R_work 0.195, R_free 0.227
Space group: P 21 21 21
Cell: a = 78.1, b = 91.3, c = 97.6 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 66.3 kDa · 600 residues in 2 chains · 3,403 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 210r
Timeline: Collected Aug 2012, deposited May 2020, released Oct 2020 · 8.2 years from beam to release
Validation: Clashscore 1.5 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: Structural basis for nuclear import selectivity of pioneer transcription factor SOX2. (Nat Commun, 2021) · cited 40 times (OpenAlex)
What came after: 61 later structures of Importin subunit alpha-1 in the PDB

PDBe PDBe-KB (P48431)PDBe-KB (P52293)UniProt P48431 UniProt P52293 AlphaFold P52293 PDB-REDO Validation report RCSB PDB

6YB7SARS-CoV-2 main protease with unliganded active site (2019-nCoV, coronavirus disease 2019, COVID-19).2020 · 1.25 Å

Protein: 3C-like proteinase (Severe acute respiratory syndrome coronavirus 2)
Resolution: 1.25 Å · R_work 0.142, R_free 0.180
Space group: C 1 2 1
Cell: a = 112.4, b = 52.8, c = 44.6 Å; α = 90.0, β = 103.0, γ = 90.0°
Size: 34.4 kDa · 305 residues in 1 chain · 2,962 atoms
Ligands: DMS, PEG
Data: Diamond, I04-1 · 0.91260 Å · DECTRIS PILATUS3 6M
Timeline: Collected Feb 2020, deposited Mar 2020, released Mar 2020 · 30 days from beam to release
Validation: Clashscore 2.5 · Ramachandran outliers 0.3% · rotamer outliers 0.0%
Paper: Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease. (Nat Commun, 2020) · cited 547 times (OpenAlex)
What came after: 1,704 later structures of 3C-like proteinase in the PDB

PDBe PDBe-KB UniProt PDB-REDO Validation report RCSB PDB

6Y84SARS-CoV-2 main protease with unliganded active site (2019-nCoV, coronavirus disease 2019, COVID-19)2020 · 1.39 Å · featured

Protein: 3C-like proteinase nsp5 (Severe acute respiratory syndrome coronavirus 2)
Resolution: 1.39 Å · R_work 0.178, R_free 0.200
Space group: C 1 2 1
Cell: a = 112.8, b = 52.9, c = 44.6 Å; α = 90.0, β = 103.2, γ = 90.0°
Size: 34.1 kDa · 306 residues in 1 chain · 2,950 atoms
Ligands: DMS
Data: Diamond, I04-1 · 0.9126 Å · DECTRIS PILATUS3 6M
Timeline: Collected Feb 2020, deposited Mar 2020, released Mar 2020 · 16 days from beam to release
Validation: Clashscore 3.5 · Ramachandran outliers 0.3% · rotamer outliers 0.0%
Paper: Crystallographic and electrophilic fragment screening of the SARS-CoV-2 main protease. (Nat Commun, 2020) · cited 547 times (OpenAlex)
What came after: 1,774 later structures of 3C-like proteinase nsp5 in the PDB

PDBe PDBe-KB UniProt PDB-REDO Validation report RCSB PDB Story and video

6VZ6Methanococcoides burtonii cytochrome b5 domain protein (WP 011499504.1)2020 · 2.1 Å

Protein: Cytochrome b5-domain protein (Methanococcoides burtonii)
Resolution: 2.1 Å · R_work 0.162, R_free 0.195
Space group: P 41 2 2
Cell: a = 67.5, b = 67.5, c = 48.1 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 9.4 kDa · 78 residues in 1 chain · 726 atoms
Ligands: HEM
Data: Australian Synchrotron, MX2 · 0.95370 Å · DECTRIS EIGER X 16M
Timeline: Collected Mar 2019, deposited Feb 2020, released Mar 2020 · 11 months from beam to release
Validation: Clashscore 4.8 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Structural characterisation of a MAPR-related archaeal cytochrome b5M protein. (FEBS Lett, 2022)
What came after: 0 later structures of Cytochrome b5-domain protein in the PDB

PDBe PDBe-KB UniProt AlphaFold PDB-REDO Validation report RCSB PDB

6PZNPutative SDR from Acinetobacter baumannii Crystal Form 22019 · 2 Å

Protein: 3-ketoacyl-ACP reductase (Acinetobacter baumannii)
Resolution: 2 Å · R_work 0.186, R_free 0.223
Space group: P 21 21 21
Cell: a = 87.6, b = 90.0, c = 130.5 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 113.9 kDa · 1,076 residues in 4 chains · 7,678 atoms
Data: Australian Synchrotron, MX2 · 0.95373 Å · DECTRIS EIGER X 16M
Timeline: Collected Feb 2018, deposited Aug 2019, released Aug 2019 · 18 months from beam to release
Validation: Clashscore 2.5 · Ramachandran outliers 0.0% · rotamer outliers 0.1%
Paper: Structural characterization of a short-chain dehydrogenase/reductase from multi-drug resistant Acinetobacter baumannii. (Biochem.Biophys.Res.Commun., 2019) · cited 8 times (OpenAlex)
What came after: 0 later structures of 3-ketoacyl-ACP reductase in the PDB

PDBe PDBe-KB UniProt AlphaFold PDB-REDO Validation report RCSB PDB

6PZMPutative SDR from Acinetobacter baumannii Crystal Form 12019 · 2.1 Å

Protein: 3-ketoacyl-ACP reductase (Acinetobacter baumannii)
Resolution: 2.1 Å · R_work 0.187, R_free 0.217
Space group: P 21 21 21
Cell: a = 80.1, b = 122.0, c = 124.7 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 113.9 kDa · 1,076 residues in 4 chains · 7,500 atoms
Data: Australian Synchrotron, MX2 · 0.9536 Å · DECTRIS EIGER X 16M
Timeline: Collected Feb 2018, deposited Aug 2019, released Aug 2019 · 18 months from beam to release
Validation: Clashscore 2.0 · Ramachandran outliers 0.0% · rotamer outliers 0.1%
Paper: Structural characterization of a short-chain dehydrogenase/reductase from multi-drug resistant Acinetobacter baumannii. (Biochem.Biophys.Res.Commun., 2019) · cited 8 times (OpenAlex)
What came after: 0 later structures of 3-ketoacyl-ACP reductase in the PDB

PDBe PDBe-KB UniProt AlphaFold PDB-REDO Validation report RCSB PDB

6Q45F1-ATPase from Fusobacterium nucleatum2019 · 3.6 Å · featured

Proteins: ATP synthase epsilon chain (Fusobacterium nucleatum subsp. nucleatum ATCC 25586); ATP synthase gamma chain (Fusobacterium nucleatum subsp. nucleatum ATCC 25586); ATP synthase subunit beta (Fusobacterium nucleatum subsp. nucleatum ATCC 25586); ATP synthase subunit alpha (Fusobacterium nucleatum subsp. nucleatum ATCC 25586)
Resolution: 3.6 Å · R_work 0.237, R_free 0.280
Space group: P 1 21 1
Cell: a = 111.9, b = 200.2, c = 201.7 Å; α = 90.0, β = 102.2, γ = 90.0°
Size: 730.3 kDa · 6,604 residues in 16 chains · 49,762 atoms
Ligands: ADP, ATP, MG
Data: Australian Synchrotron, MX2 · 0.954 Å · ADSC QUANTUM 315r
Timeline: Collected Oct 2015, deposited Dec 2018, released July 2019 · 3.7 years from beam to release
Validation: Clashscore 1.4 · Ramachandran outliers 0.3% · rotamer outliers 1.2%
Paper: Structure of F1-ATPase from the obligate anaerobe Fusobacterium nucleatum. (Open Biology, 2019) · cited 6 times (OpenAlex)
What came after: 0 later structures of ATP synthase epsilon chain in the PDB; 0 later structures of ATP synthase gamma chain in the PDB; 0 later structures of ATP synthase subunit beta in the PDB; 0 later structures of ATP synthase subunit alpha in the PDB

PDBe PDBe-KB (Q8RGE3)PDBe-KB (Q8RGE1)PDBe-KB (Q8RGE2)PDBe-KB (Q8RGE0)UniProt Q8RGE3 UniProt Q8RGE1 UniProt Q8RGE2 UniProt Q8RGE0 AlphaFold Q8RGE3 AlphaFold Q8RGE1 AlphaFold Q8RGE2 AlphaFold Q8RGE0 PDB-REDO Validation report RCSB PDB Story and video

6NZXHadesarchaea YNP_N21 cytochrome b5 domain protein (KUO41884.1)2019 · 1.9 Å

Protein: Cytochrome B5 (Hadesarchaea archaeon YNP_N21)
Resolution: 1.9 Å · R_work 0.221, R_free 0.261
Space group: P 63
Cell: a = 72.2, b = 72.2, c = 22.8 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 9.2 kDa · 78 residues in 1 chain · 663 atoms
Ligands: HEM
Data: Australian Synchrotron, MX2 · 0.95370 Å · DECTRIS EIGER X 16M
Timeline: Collected June 2018, deposited Feb 2019, released Mar 2019 · 9 months from beam to release
Validation: Clashscore 4.8 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Structural characterisation of a MAPR-related archaeal cytochrome b5M protein. (FEBS Lett, 2022)

PDBe PDB-REDO Validation report RCSB PDB

6NRPPutative short-chain dehydrogenase/reductase (SDR) from Acinetobacter baumannii2019 · 1.9 Å

Protein: 3-oxoacyl-ACP reductase FabG (Acinetobacter baumannii)
Resolution: 1.9 Å · R_work 0.170, R_free 0.192
Space group: P 31 2 1
Cell: a = 89.5, b = 89.5, c = 239.5 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 114.9 kDa · 1,052 residues in 4 chains · 7,616 atoms
Data: Australian Synchrotron, MX2 · 0.95372 Å · DECTRIS EIGER X 16M
Timeline: Collected Feb 2018, deposited Jan 2019, released Feb 2019 · 12 months from beam to release
Validation: Clashscore 2.8 · Ramachandran outliers 0.0% · rotamer outliers 0.4%
Paper: Insights into Acinetobacter baumannii fatty acid synthesis 3-oxoacyl-ACP reductases. (Sci Rep, 2021) · cited 25 times (OpenAlex)

PDBe PDB-REDO Validation report RCSB PDB

6BWBHendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 32018 · 2.3 Å

Proteins: Protein W (Hendra virus); Importin subunit alpha-3 (Homo sapiens)
Resolution: 2.3 Å · R_work 0.178, R_free 0.218
Space group: P 21 21 21
Cell: a = 48.2, b = 59.0, c = 169.3 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 55.0 kDa · 500 residues in 2 chains · 3,624 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 315r
Timeline: Collected Nov 2016, deposited Dec 2017, released July 2018 · 20 months from beam to release
Validation: Clashscore 2.0 · Ramachandran outliers 0.0% · rotamer outliers 0.8%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 9 later structures of Importin subunit alpha-3 in the PDB

PDBe PDBe-KB (P0C1C6)PDBe-KB (O00629)UniProt P0C1C6 UniProt O00629 AlphaFold O00629 PDB-REDO Validation report RCSB PDB

6BWAHendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 22018 · 2.2 Å

Proteins: Protein W (Hendra virus); Importin subunit alpha-3 (Homo sapiens)
Resolution: 2.2 Å · R_work 0.187, R_free 0.216
Space group: P 1 21 1
Cell: a = 48.1, b = 60.0, c = 89.9 Å; α = 90.0, β = 97.9, γ = 90.0°
Size: 55.0 kDa · 500 residues in 2 chains · 3,678 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 315r
Timeline: Collected July 2016, deposited Dec 2017, released July 2018 · 24 months from beam to release
Validation: Clashscore 0.9 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 9 later structures of Importin subunit alpha-3 in the PDB

PDBe PDBe-KB (P0C1C6)PDBe-KB (O00629)UniProt P0C1C6 UniProt O00629 AlphaFold O00629 PDB-REDO Validation report RCSB PDB

6BW9Hendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 12018 · 1.6 Å · featured

Proteins: Protein W (Hendra virus); Importin subunit alpha-3 (Homo sapiens)
Resolution: 1.6 Å · R_work 0.171, R_free 0.196
Space group: P 1 21 1
Cell: a = 47.4, b = 65.7, c = 74.2 Å; α = 90.0, β = 99.8, γ = 90.0°
Size: 55.0 kDa · 500 residues in 2 chains · 3,738 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 315r
Timeline: Collected Nov 2016, deposited Dec 2017, released July 2018 · 20 months from beam to release
Validation: Clashscore 2.1 · Ramachandran outliers 0.0% · rotamer outliers 0.5%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 9 later structures of Importin subunit alpha-3 in the PDB

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6BW1Hendra virus W protein C-terminus in complex with Importin alpha 12018 · 2.2 Å

Proteins: Importin subunit alpha-1 (Mus musculus); Protein W (Hendra virus)
Resolution: 2.2 Å · R_work 0.192, R_free 0.212
Space group: P 21 21 21
Cell: a = 79.0, b = 89.3, c = 100.4 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 60.0 kDa · 551 residues in 2 chains · 3,431 atoms
Data: Australian Synchrotron, MX1 · 0.9537 Å · ADSC QUANTUM 210r
Timeline: Collected June 2016, deposited Dec 2017, released July 2018 · 2.1 years from beam to release
Validation: Clashscore 1.2 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 75 later structures of Importin subunit alpha-1 in the PDB

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6BW0Nipah virus W protein C-terminus in complex with Importin alpha 12018 · 2.1 Å

Proteins: Importin subunit alpha-1 (Mus musculus); Protein W (Nipah virus)
Resolution: 2.1 Å · R_work 0.186, R_free 0.203
Space group: P 21 21 21
Cell: a = 77.9, b = 88.8, c = 97.6 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 60.0 kDa · 551 residues in 2 chains · 3,555 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Mar 2017, deposited Dec 2017, released July 2018 · 16 months from beam to release
Validation: Clashscore 0.8 · Ramachandran outliers 0.0% · rotamer outliers 1.4%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 75 later structures of Importin subunit alpha-1 in the PDB

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6BVZImportin alpha 3 in cargo free state2018 · 2.3 Å

Protein: Importin subunit alpha-3 (Homo sapiens)
Resolution: 2.3 Å · R_work 0.250, R_free 0.269
Space group: P 1 21 1
Cell: a = 47.1, b = 53.2, c = 91.3 Å; α = 90.0, β = 92.9, γ = 90.0°
Size: 50.3 kDa · 459 residues in 1 chain · 3,210 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Apr 2017, deposited Dec 2017, released July 2018 · 15 months from beam to release
Validation: Clashscore 4.0 · Ramachandran outliers 0.0% · rotamer outliers 0.8%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 9 later structures of Importin subunit alpha-3 in the PDB

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6BVVNipah virus W protein C-terminus in complex with Importin alpha 32018 · 2.3 Å

Proteins: Protein W (Nipah virus); Importin subunit alpha-3 (Homo sapiens)
Resolution: 2.3 Å · R_work 0.199, R_free 0.222
Space group: P 1 21 1
Cell: a = 47.7, b = 65.6, c = 73.9 Å; α = 90.0, β = 99.8, γ = 90.0°
Size: 55.1 kDa · 500 residues in 2 chains · 3,592 atoms
Data: Australian Synchrotron, MX2 · 0.9537 Å · DECTRIS EIGER X 16M
Timeline: Collected Mar 2017, deposited Dec 2017, released July 2018 · 16 months from beam to release
Validation: Clashscore 1.0 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 9 later structures of Importin subunit alpha-3 in the PDB

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6BVTImportin alpha 1 in cargo free state2018 · 2.5 Å

Protein: Importin subunit alpha-1 (Mus musculus)
Resolution: 2.5 Å · R_work 0.192, R_free 0.213
Space group: P 21 21 21
Cell: a = 78.5, b = 90.0, c = 100.7 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 55.3 kDa · 510 residues in 1 chain · 3,361 atoms
Data: Australian Synchrotron, MX1 · 0.9537 Å · ADSC QUANTUM 315r
Timeline: Collected Mar 2016, deposited Dec 2017, released July 2018 · 2.3 years from beam to release
Validation: Clashscore 0.5 · Ramachandran outliers 0.0% · rotamer outliers 0.8%
Paper: Structural basis for importin alpha 3 specificity of W proteins in Hendra and Nipah viruses. (Nat Commun, 2018) · cited 75 times (OpenAlex)
What came after: 75 later structures of Importin subunit alpha-1 in the PDB

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6BDOStructure of bacterial type II NADH dehydrogenase from Caldalkalibacillus thermarum complexed with a quinone inhibitor HQNO at 2.8A resolution2018 · 2.8 Å

Protein: FAD-dependent pyridine nucleotide-disulfide oxidoreductase (Caldalkalibacillus thermarum TA2.A1)
Resolution: 2.8 Å · R_work 0.227, R_free 0.268
Space group: P 1 21 1
Cell: a = 72.8, b = 114.3, c = 130.1 Å; α = 90.0, β = 91.2, γ = 90.0°
Size: 182.0 kDa · 1,620 residues in 4 chains · 11,896 atoms
Ligands: FAD, HQO
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 315r
Timeline: Collected Nov 2016, deposited Oct 2017, released May 2018 · 18 months from beam to release
Validation: Clashscore 4.6 · Ramachandran outliers 0.2% · rotamer outliers 2.1%
Paper: Structure of the NDH-2 - HQNO inhibited complex provides molecular insight into quinone-binding site inhibitors. (Biochim. Biophys. Acta, 2018) · cited 48 times (OpenAlex)
What came after: 0 later structures of FAD-dependent pyridine nucleotide-disulfide oxidoreductase in the PDB

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5WEDStructure of bacterial type II NADH dehydrogenase from Caldalkalibacillus thermarum at 2.15A resolution2017 · 2.15 Å

Protein: FAD-dependent pyridine nucleotide-disulfide oxidoreductase (Caldalkalibacillus thermarum TA2.A1)
Resolution: 2.15 Å · R_work 0.208, R_free 0.238
Space group: P 1 21 1
Cell: a = 72.8, b = 113.6, c = 129.8 Å; α = 90.0, β = 91.0, γ = 90.0°
Size: 181.4 kDa · 1,620 residues in 4 chains · 12,435 atoms
Ligands: FAD
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 315r
Timeline: Collected Oct 2015, deposited July 2017, released Oct 2017 · 24 months from beam to release
Validation: Clashscore 1.4 · Ramachandran outliers 0.0% · rotamer outliers 0.1%
Paper: Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 angstrom. (Acta Crystallogr F Struct Biol Commun, 2017) · cited 15 times (OpenAlex)
What came after: 1 later structure of FAD-dependent pyridine nucleotide-disulfide oxidoreductase in the PDB

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5KMSThe structure of type II NADH dehydrogenase from Caldalkalibacillus thermarum complexed with NAD+ at 2.5 angstrom resolution.2017 · 2.5 Å

Protein: FAD-dependent pyridine nucleotide-disulfide oxidoreductase (Caldalkalibacillus thermarum TA2.A1)
Resolution: 2.5 Å · R_work 0.214, R_free 0.244
Space group: P 1 21 1
Cell: a = 72.9, b = 114.0, c = 130.6 Å; α = 90.0, β = 91.8, γ = 90.0°
Size: 182.1 kDa · 1,620 residues in 4 chains · 11,969 atoms
Ligands: FAD, NAD
Data: Australian Synchrotron, MX2 · 0.954 Å · ADSC QUANTUM 315r
Timeline: Collected Oct 2015, deposited June 2016, released Feb 2017 · 15 months from beam to release
Validation: Clashscore 2.4 · Ramachandran outliers 0.3% · rotamer outliers 2.4%
Paper: The mechanism of catalysis by type-II NADH:quinone oxidoreductases. (Sci Rep, 2017) · cited 80 times (OpenAlex)
What came after: 2 later structures of FAD-dependent pyridine nucleotide-disulfide oxidoreductase in the PDB

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5KMRThe structure of type II NADH dehydrogenase from Caldalkalibacillus thermarum complexed with NAD+ at 3.0 angstrom resolution.2017 · 3 Å · featured

Protein: FAD-dependent pyridine nucleotide-disulfide oxidoreductase (Caldalkalibacillus thermarum TA2.A1)
Resolution: 3 Å · R_work 0.237, R_free 0.254
Space group: P 1 21 1
Cell: a = 72.1, b = 114.2, c = 131.0 Å; α = 90.0, β = 91.5, γ = 90.0°
Size: 183.4 kDa · 1,620 residues in 4 chains · 11,468 atoms
Ligands: FAD, NAD
Data: Australian Synchrotron, MX2 · 0.954 Å · ADSC QUANTUM 315r
Timeline: Collected Oct 2015, deposited June 2016, released Jan 2017 · 15 months from beam to release
Validation: Clashscore 5.5 · Ramachandran outliers 0.8% · rotamer outliers 1.7%
Paper: The mechanism of catalysis by type-II NADH:quinone oxidoreductases. (Sci Rep, 2017) · cited 80 times (OpenAlex)
What came after: 3 later structures of FAD-dependent pyridine nucleotide-disulfide oxidoreductase in the PDB

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5KMQThe structure of I379E variant of type II NADH dehydrogenase from Caldalkalibacillus thermarum2017 · 2.7 Å

Protein: FAD-dependent pyridine nucleotide-disulfide oxidoreductase (Caldalkalibacillus thermarum TA2.A1)
Resolution: 2.7 Å · R_work 0.223, R_free 0.269
Space group: P 1 21 1
Cell: a = 72.4, b = 114.4, c = 130.5 Å; α = 90.0, β = 92.0, γ = 90.0°
Size: 181.5 kDa · 1,620 residues in 4 chains · 11,334 atoms
Ligands: FAD
Data: Australian Synchrotron, MX2 · 0.954 Å · ADSC QUANTUM 315r
Timeline: Collected Oct 2015, deposited June 2016, released Jan 2017 · 15 months from beam to release
Validation: Clashscore 4.0 · Ramachandran outliers 0.3% · rotamer outliers 3.5%
Paper: The mechanism of catalysis by type-II NADH:quinone oxidoreductases. (Sci Rep, 2017) · cited 80 times (OpenAlex)
What came after: 3 later structures of FAD-dependent pyridine nucleotide-disulfide oxidoreductase in the PDB

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5KMPThe structure of G164E variant of type II NADH dehydrogenase from Caldalkalibacillus thermarum2017 · 3.2 Å

Protein: FAD-dependent pyridine nucleotide-disulfide oxidoreductase (Caldalkalibacillus thermarum TA2.A1)
Resolution: 3.2 Å · R_work 0.203, R_free 0.234
Space group: P 41 21 2
Cell: a = 93.1, b = 93.1, c = 248.5 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 90.9 kDa · 810 residues in 2 chains · 5,679 atoms
Ligands: FAD
Data: Australian Synchrotron, MX2 · 0.954 Å · ADSC QUANTUM 315r
Timeline: Collected Nov 2015, deposited June 2016, released Jan 2017 · 15 months from beam to release
Validation: Clashscore 7.9 · Ramachandran outliers 0.3% · rotamer outliers 6.1%
Paper: The mechanism of catalysis by type-II NADH:quinone oxidoreductases. (Sci Rep, 2017) · cited 80 times (OpenAlex)
What came after: 3 later structures of FAD-dependent pyridine nucleotide-disulfide oxidoreductase in the PDB

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5J37Crystal structure of 60-mer BFDV Capsid Protein in complex with single stranded DNA2016 · 2.3 Å

Proteins: single stranded DNA (synthetic construct); Beak and feather disease virus capsid protein (Beak and feather disease virus)
Resolution: 2.3 Å · R_work 0.174, R_free 0.197
Space group: F 4 3 2
Cell: a = 377.3, b = 377.3, c = 377.3 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 197.2 kDa · 1,435 residues in 10 chains · 9,275 atoms
Ligands: PO4
Data: Australian Synchrotron, MX2 · 0.9537 Å · ADSC QUANTUM 315r
Timeline: Collected Oct 2015, deposited Mar 2016, released May 2016 · 7 months from beam to release
Validation: Clashscore 1.1 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Structural insights into the assembly and regulation of distinct viral capsid complexes. (Nat Commun, 2016) · cited 79 times (OpenAlex)
What came after: 0 later structures of Capsid protein in the PDB

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5J36Crystal structure of 60-mer BFDV Capsid Protein2016 · 2.55 Å · featured

Protein: Beak and feather disease virus capsid protein (Beak and feather disease virus)
Resolution: 2.55 Å · R_work 0.191, R_free 0.216
Space group: F 4 3 2
Cell: a = 377.3, b = 377.3, c = 377.3 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 151.7 kDa · 1,285 residues in 5 chains · 8,662 atoms
Ligands: PO4
Data: Australian Synchrotron, MX2 · 1 Å · ADSC QUANTUM 315r
Timeline: Collected Oct 2015, deposited Mar 2016, released May 2016 · 7 months from beam to release
Validation: Clashscore 0.7 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: Structural insights into the assembly and regulation of distinct viral capsid complexes. (Nat Commun, 2016) · cited 79 times (OpenAlex)
What came after: 0 later structures of Capsid protein in the PDB

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5J09Crystal structure of decameric BFDV Capsid Protein2016 · 2 Å

Protein: Beak and feather disease virus capsid protein (Beak and feather disease virus)
Resolution: 2 Å · R_work 0.209, R_free 0.239
Space group: P 21 21 21
Cell: a = 78.8, b = 148.4, c = 188.6 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 302.4 kDa · 2,570 residues in 10 chains · 15,272 atoms
Data: Australian Synchrotron, MX2 · 0.95370 Å · ADSC QUANTUM 315
Timeline: Collected Jan 2015, deposited Mar 2016, released May 2016 · 16 months from beam to release
Validation: Clashscore 1.3 · Ramachandran outliers 0.0% · rotamer outliers 0.6%
Paper: Structural insights into the assembly and regulation of distinct viral capsid complexes. (Nat Commun, 2016) · cited 79 times (OpenAlex)
What came after: 0 later structures of Capsid protein in the PDB

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4UXWStructure of delta4-DgkA-apo in 9.9 MAG2015 · 3.15 Å

Protein: Diacylglycerol kinase (ESCHERICHIA COLI K-12)
Resolution: 3.15 Å · R_work 0.224, R_free 0.268
Space group: P 31 2 1
Cell: a = 72.8, b = 72.8, c = 199.3 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 45.1 kDa · 390 residues in 3 chains · 2,754 atoms
Ligands: MPD, NA, NO3, OLC
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected July 2011, deposited Aug 2014, released Sept 2015 · 4.2 years from beam to release
Validation: Clashscore 9.3 · Ramachandran outliers 0.0% · rotamer outliers 3.0%
Paper: Ternary Structure Reveals Mechanism of a Membrane Diacylglycerol Kinase. (Nat.Commun., 2015) · cited 43 times (OpenAlex)
What came after: 5 later structures of Diacylglycerol kinase in the PDB

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4CK0Crystal structure of the integral membrane diacylglycerol kinase - form 22015 · 2.924 Å

Protein: Diacylglycerol kinase (ESCHERICHIA COLI)
Resolution: 2.924 Å · R_work 0.248, R_free 0.281
Space group: P 31 2 1
Cell: a = 72.8, b = 72.8, c = 195.7 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 44.1 kDa · 390 residues in 3 chains · 2,647 atoms
Ligands: ACP, OLC, ZN
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected Dec 2012, deposited Dec 2013, released Jan 2015 · 2.2 years from beam to release
Validation: Clashscore 4.3 · Ramachandran outliers 0.0% · rotamer outliers 1.5%
Paper: The PDB entry isn't linked to a published paper yet.
What came after: 9 later structures of Diacylglycerol kinase in the PDB

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4CJZCrystal structure of the integral membrane diacylglycerol kinase DgkA- 9.9, delta 42015 · 3.25 Å

Protein: Diacylglycerol kinase (ESCHERICHIA COLI)
Resolution: 3.25 Å · R_work 0.255, R_free 0.292
Space group: P 31 2 1
Cell: a = 72.8, b = 72.8, c = 199.3 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 43.1 kDa · 390 residues in 3 chains · 2,596 atoms
Ligands: OLC
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected July 2011, deposited Dec 2013, released Jan 2015 · 3.5 years from beam to release
Validation: Clashscore 2.8 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: The PDB entry isn't linked to a published paper yet.
What came after: 9 later structures of Diacylglycerol kinase in the PDB

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4B61In meso structure of alginate transporter, AlgE, from Pseudomoas aeruginosa, PAO1. Crystal form 3.2013 · 2.402 Å

Protein: Alginate production protein alge (PSEUDOMONAS AERUGINOSA PAO1)
Resolution: 2.402 Å · R_work 0.221, R_free 0.244
Space group: P 21 21 21
Cell: a = 61.7, b = 77.5, c = 240.3 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 110.5 kDa · 916 residues in 2 chains · 7,509 atoms
Ligands: 78M, 78N, ACT, CU, LDA, MG
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected June 2009, deposited Aug 2012, released July 2013 · 4.1 years from beam to release
Validation: Clashscore 5.8 · Ramachandran outliers 0.0% · rotamer outliers 1.6%
Paper: A Conformational Landscape for Alginate Secretion Across the Outer Membrane of Pseudomonas Aeruginosa. (Acta Crystallogr.,Sect.D, 2014) · cited 53 times (OpenAlex)
What came after: 8 later structures of Alginate production protein AlgE in the PDB

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4AZLIn meso structure of alginate transporter, AlgE, from Pseudomoas aeruginosa, PAO1, crystal form 2.2013 · 2.8 Å

Protein: Alginate production protein alge (PSEUDOMONAS AERUGINOSA)
Resolution: 2.8 Å · R_work 0.237, R_free 0.280
Space group: P 1 21 1
Cell: a = 47.1, b = 245.8, c = 47.1 Å; α = 90.0, β = 104.4, γ = 90.0°
Size: 106.6 kDa · 916 residues in 2 chains · 6,941 atoms
Ligands: 78M, 78N, CA
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected Mar 2010, deposited June 2012, released July 2013 · 3.3 years from beam to release
Validation: Clashscore 4.3 · Ramachandran outliers 0.0% · rotamer outliers 1.2%
Paper: A Conformational Landscape for Alginate Secretion Across the Outer Membrane of Pseudomonas Aeruginosa. (Acta Crystallogr.,Sect.D, 2014) · cited 53 times (OpenAlex)
What came after: 9 later structures of Alginate production protein AlgE in the PDB

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3ZE5Crystal structure of the integral membrane diacylglycerol kinase - delta42013 · 3.101 Å

Protein: Diacylglycerol kinase (ESCHERICHIA COLI K-12)
Resolution: 3.101 Å · R_work 0.232, R_free 0.258
Space group: P 31 2 1
Cell: a = 72.7, b = 72.7, c = 199.0 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 42.7 kDa · 390 residues in 3 chains · 2,569 atoms
Data: Diamond, I24 · DECTRIS PILATUS 6M
Timeline: Collected Dec 2010, deposited Dec 2012, released May 2013 · 2.4 years from beam to release
Validation: Clashscore 2.9 · Ramachandran outliers 0.0% · rotamer outliers 0.4%
Paper: Crystal Structure of the Integral Membrane Diacylglycerol Kinase. (Nature, 2013) · cited 95 times (OpenAlex)
What came after: 16 later structures of Diacylglycerol kinase in the PDB

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3ZE4Crystal structure of the integral membrane diacylglycerol kinase - wild-type2013 · 3.702 Å

Protein: Diacylglycerol kinase (ESCHERICHIA COLI K-12)
Resolution: 3.702 Å · R_work 0.285, R_free 0.312
Space group: P 31 2 1
Cell: a = 75.0, b = 75.0, c = 196.9 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 42.8 kDa · 390 residues in 3 chains · 2,458 atoms
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected June 2012, deposited Dec 2012, released May 2013 · 11 months from beam to release
Validation: Clashscore 7.0 · Ramachandran outliers 0.0% · rotamer outliers 2.0%
Paper: Crystal Structure of the Integral Membrane Diacylglycerol Kinase. (Nature, 2013) · cited 95 times (OpenAlex)
What came after: 16 later structures of Diacylglycerol kinase in the PDB

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3ZE3Crystal structure of the integral membrane diacylglycerol kinase - delta72013 · 2.05 Å · featured

Protein: Diacylglycerol kinase (ESCHERICHIA COLI K-12)
Resolution: 2.05 Å · R_work 0.196, R_free 0.217
Space group: P 21 21 21
Cell: a = 75.1, b = 91.5, c = 143.7 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 89.7 kDa · 780 residues in 6 chains · 5,042 atoms
Ligands: 78M, 78N, ACT, FLC, NA, ZN
Data: Advanced Photon Source, 23-ID-B · 1.03320, 0.97944 Å · MARRESEARCH
Timeline: Collected June 2012, deposited Dec 2012, released May 2013 · 11 months from beam to release
Validation: Clashscore 4.1 · Ramachandran outliers 0.0% · rotamer outliers 1.1%
Paper: Crystal Structure of the Integral Membrane Diacylglycerol Kinase. (Nature, 2013) · cited 95 times (OpenAlex)
What came after: 16 later structures of Diacylglycerol kinase in the PDB

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4AFKIn meso structure of alginate transporter, AlgE, from Pseudomonas aeruginosa, PAO12013 · 1.897 Å · featured

Protein: Alginate production protein alge (PSEUDOMONAS AERUGINOSA)
Resolution: 1.897 Å · R_work 0.163, R_free 0.209
Space group: C 1 2 1
Cell: a = 57.3, b = 74.4, c = 115.5 Å; α = 90.0, β = 101.6, γ = 90.0°
Size: 57.6 kDa · 458 residues in 1 chain · 4,073 atoms
Ligands: 78M, 78N, CA, FLC, LDA, NA, PE5
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected Apr 2008, deposited Jan 2012, released Feb 2013 · 4.8 years from beam to release
Validation: Clashscore 6.8 · Ramachandran outliers 0.0% · rotamer outliers 0.3%
Paper: A Conformational Landscape for Alginate Secretion Across the Outer Membrane of Pseudomonas Aeruginosa. (Acta Crystallogr.,Sect.D, 2014) · cited 53 times (OpenAlex)
What came after: 10 later structures of Alginate production protein AlgE in the PDB

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3ZQ8STRUCTURE OF LINEAR GRAMICIDIN D OBTAINED USING TYPE I CRYSTALS GROWN IN A monovaccenin LIPID CUBIC PHASE2012 · 1.7 Å

Protein: Val-gramicidin a (BREVIBACILLUS BREVIS)
Resolution: 1.7 Å · R_work 0.166, R_free 0.211
Space group: P 1 21 1
Cell: a = 24.0, b = 42.0, c = 32.4 Å; α = 90.0, β = 107.3, γ = 90.0°
Size: 8.6 kDa · 64 residues in 4 chains · 633 atoms
Ligands: MVC
Data: ESRF, ID14-4 · ADSC QUANTUM 315r
Timeline: Collected Oct 2009, deposited June 2011, released July 2012 · 2.8 years from beam to release
Validation: Clashscore 7.2 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: The PDB entry isn't linked to a published paper yet.

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2YEVStructure of caa3-type cytochrome oxidase2012 · 2.36 Å · featured

Proteins: Caa3-type cytochrome oxidase subunit iv (THERMUS THERMOPHILUS); Cytochrome c oxidase subunit 2 (THERMUS THERMOPHILUS); Cytochrome c oxidase polypeptide i+iii (THERMUS THERMOPHILUS)
Resolution: 2.36 Å · R_work 0.171, R_free 0.218
Space group: I 1 2 1
Cell: a = 127.3, b = 76.0, c = 300.3 Å; α = 90.0, β = 92.2, γ = 90.0°
Size: 277.4 kDa · 2,388 residues in 6 chains · 19,587 atoms
Ligands: 4AG, 5PL, 7E8, 7E9, CL, CU, CUA, HAS, HEC, MG
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected June 2010, deposited Mar 2011, released May 2012 · 23 months from beam to release
Validation: Clashscore 6.0 · Ramachandran outliers 0.0% · rotamer outliers 0.9%
Paper: Structural Insights Into Electron Transfer in Caa3-Type Cytochrome Oxidases. (Nature, 2012) · cited 126 times (OpenAlex)
What came after: 0 later structures of Cytochrome oxidase Caa3-type subunit IV domain-containing protein in the PDB; 0 later structures of Cytochrome c oxidase subunit 2 in the PDB; 0 later structures of Cytochrome c oxidase polypeptide I+III in the PDB

PDBe PDBe-KB (Q5SH67)PDBe-KB (Q5SLI2)PDBe-KB (P98005)UniProt Q5SH67 UniProt Q5SLI2 UniProt P98005 AlphaFold Q5SH67 AlphaFold Q5SLI2 AlphaFold P98005 PDB-REDO Validation report RCSB PDB Story and video

2Y6NStructure of linear gramicidin d obtained using type i crystals grown in a 8.8 monoacylglycerol lipid cubic phase.2011 · 1.26 Å

Protein: Val-gramicidin a (BREVIBACILLUS BREVIS)
Resolution: 1.26 Å · R_work 0.148, R_free 0.170
Space group: P 1 21 1
Cell: a = 30.6, b = 62.8, c = 30.6 Å; α = 90.0, β = 100.0, γ = 90.0°
Size: 16.2 kDa · 96 residues in 6 chains · 974 atoms
Ligands: 15P, P4C
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH MX-300
Timeline: Collected Feb 2009, deposited Jan 2011, released May 2011 · 2.2 years from beam to release
Validation: Clashscore 7.7 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Membrane Protein Crystallization in Lipidic Mesophases. Hosting Lipid Effects on the Crystallization and Structure of a Transmembrane Peptide (Cryst.Growth Des., 2011) · cited 33 times (OpenAlex)

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2Y5MStructure of linear gramicidin d obtained using type i crystals grown in a 7.7 monoacylglycerol lipid cubic phase.2011 · 1.08 Å · featured

Protein: Val-gramicidin a (BREVIBACILLUS BREVIS)
Resolution: 1.08 Å · R_work 0.130, R_free 0.155
Space group: P 1 21 1
Cell: a = 30.6, b = 62.8, c = 30.7 Å; α = 90.0, β = 100.0, γ = 90.0°
Size: 15.9 kDa · 96 residues in 6 chains · 966 atoms
Ligands: 15P
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH MX-300
Timeline: Collected Aug 2008, deposited Jan 2011, released May 2011 · 2.8 years from beam to release
Validation: Clashscore 3.1 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Membrane Protein Crystallization in Lipidic Mesophases. Hosting Lipid Effects on the Crystallization and Structure of a Transmembrane Peptide (Cryst.Growth Des., 2011) · cited 33 times (OpenAlex)

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3PDSIrreversible Agonist-Beta2 Adrenoceptor Complex2011 · 3.5 Å · featured

Protein: Fusion protein Beta-2 adrenergic receptor/Lysozyme (Homo sapiens)
Resolution: 3.5 Å · R_work 0.238, R_free 0.283
Space group: P 21 21 2
Cell: a = 282.4, b = 40.0, c = 65.2 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 53.9 kDa · 458 residues in 1 chain · 3,628 atoms
Ligands: CLR, ERC, SO4
Data: Advanced Photon Source, 23-ID-B · 1.033 Å · MARMOSAIC 300 mm CCD
Timeline: Collected June 2010, deposited Oct 2010, released Jan 2011 · 6 months from beam to release
Validation: Clashscore 2.5 · Ramachandran outliers 0.2% · rotamer outliers 4.2%
Paper: Structure and function of an irreversible agonist-beta(2) adrenoceptor complex (Nature, 2011) · cited 784 times (OpenAlex)
What came after: 139 later structures of Beta-2 adrenergic receptor in the PDB

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2XDCStructure of linear gramicidin D obtained using Type I crystals grown in a lipid cubic phase.2010 · 1.7 Å

Protein: Gramicidin a (BREVIBACILLUS BREVIS)
Resolution: 1.7 Å · R_work 0.179, R_free 0.214
Space group: P 1 21 1
Cell: a = 30.5, b = 62.6, c = 30.5 Å; α = 90.0, β = 100.0, γ = 90.0°
Size: 17.4 kDa · 96 residues in 6 chains · 935 atoms
Ligands: 15P, NA
Data: Advanced Photon Source, 23-ID-B · MARRESEARCH
Timeline: Collected Oct 2008, deposited Apr 2010, released Aug 2010 · 22 months from beam to release
Validation: Clashscore 2.7 · Ramachandran outliers 0.0% · rotamer outliers 0.0%
Paper: Crystallizing Transmembrane Peptides in Lipidic Mesophases (Biophys.J., 2010) · cited 44 times (OpenAlex)

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2VKR3Fe-4S, 4Fe-4S plus Zn Acidianus ambivalens ferredoxin2008 · 2.01 Å · featured

Protein: Zinc-containing ferredoxin (ACIDIANUS AMBIVALENS)
Resolution: 2.01 Å
Space group: P 31
Cell: a = 117.5, b = 117.5, c = 50.9 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 82.1 kDa · 721 residues in 7 chains · 5,616 atoms
Ligands: F3S, SF4, ZN
Data: ESRF, ID14-2 · ADSC CCD
Timeline: Collected Sept 2002, deposited Dec 2007, released Mar 2008 · 5.4 years from beam to release
Validation: Clashscore 19.5 · Ramachandran outliers 0.6% · rotamer outliers 11.3%
Paper: Crystallographic analysis of the intact metal centres [3Fe-4S](1+/0) and [4Fe-4S](2+/1+) in a Zn(2+) -containing ferredoxin. (FEBS Lett., 2008) · cited 11 times (OpenAlex)
What came after: 0 later structures of Zinc-containing ferredoxin in the PDB

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2UX8Crystal Structure of Sphingomonas elodea ATCC 31461 Glucose-1- phosphate uridylyltransferase in Complex with glucose-1-phosphate.2007 · 2.65 Å

Protein: Glucose-1-phosphate uridylyltransferase (SPHINGOMONAS ELODEA)
Resolution: 2.65 Å · R_work 0.245, R_free 0.295
Space group: P 1 21 1
Cell: a = 105.6, b = 85.7, c = 151.8 Å; α = 90.0, β = 105.2, γ = 90.0°
Size: 259.8 kDa · 2,376 residues in 8 chains · 16,948 atoms
Ligands: G1P
Data: ESRF, ID29 · 0.97564, 1.13980 Å · ADSC CCD
Timeline: Collected Sept 2005, deposited Mar 2007, released May 2007 · 20 months from beam to release
Validation: Clashscore 24.7 · Ramachandran outliers 2.2% · rotamer outliers 10.9%
Paper: The Complex of Sphingomonas Elodea Atcc 31461 Glucose-1-Phosphate Uridylyltransferase with Glucose-1-Phosphate Reveals a Novel Quaternary Structure, Unique Among Nucleoside Diphosphate-Sugar Pyrophosphorylase Members. (J.Bacteriol., 2007) · cited 33 times (OpenAlex)
What came after: 0 later structures of UTP--glucose-1-phosphate uridylyltransferase in the PDB

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1W9MAS-isolated hybrid cluster protein from Desulfovibrio vulgaris X-ray structure at 1.35A resolution using iron anomalous signal2005 · 1.35 Å · featured

Protein: Hydroxylamine reductase (DESULFOVIBRIO VULGARIS)
Resolution: 1.35 Å
Space group: P 21 21 21
Cell: a = 64.3, b = 66.8, c = 134.8 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 60.8 kDa · 553 residues in 1 chain · 5,065 atoms
Ligands: FSO, SF4
Data: ESRF, ID29 · ADSC CCD
Timeline: Collected Nov 2001, deposited Oct 2004, released Feb 2005 · 3.2 years from beam to release
Validation: Clashscore 3.0 · Ramachandran outliers 0.0% · rotamer outliers 1.4%
Paper: Structural and Functional Relationships in the Hybrid Cluster Protein Family:Structure of the Anaerobically Purified Hybrid Cluster Protein from Desulfovibrio Vulgaris at 1.35 A Resolution (Acta Crystallogr.,Sect.D, 2008) · cited 30 times (OpenAlex)
What came after: 0 later structures of Hydroxylamine reductase in the PDB

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1UPXThe crystal structure of the Hybrid Cluster Protein from Desulfovibrio desulfuricans containing molecules in the oxidized and reduced states.2003 · 1.25 Å

Protein: Hydroxylamine reductase (DESULFOVIBRIO DESULFURICANS)
Resolution: 1.25 Å · R_work 0.140, R_free 0.153
Space group: P 1
Cell: a = 57.3, b = 61.2, c = 72.0 Å; α = 82.8, β = 73.7, γ = 87.3°
Size: 119.5 kDa · 1,088 residues in 2 chains · 10,132 atoms
Ligands: FSO, MES, SF3, SF4
Data: ESRF, ID14-2 · ADSC CCD
Timeline: Collected May 2000, deposited Oct 2003, released Dec 2003 · 3.6 years from beam to release
Validation: Clashscore 3.2 · Ramachandran outliers 0.0% · rotamer outliers 1.6%
Paper: Structure of the Hybrid Cluster Protein (Hcp) from Desulfovibrio Desulfuricans Atcc 27774 Containing Molecules in the Oxidized and Reduced States (Acta Crystallogr.,Sect.D, 2003) · cited 13 times (OpenAlex)
What came after: 0 later structures of Hydroxylamine reductase in the PDB

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1OA1Reduced hybrid cluster protein (hcp) from desulfovibrio vulgaris hildenborough structure at 1.55a resolution using synchrotron radiation.2003 · 1.55 Å

Protein: Hydroxylamine reductase (DESULFOVIBRIO VULGARIS)
Resolution: 1.55 Å · R_work 0.131, R_free 0.153
Space group: P 21 21 21
Cell: a = 64.1, b = 67.5, c = 135.0 Å; α = 90.0, β = 90.0, γ = 90.0°
Size: 60.9 kDa · 553 residues in 1 chain · 5,117 atoms
Ligands: GOL, SF3, SF4
Data: ESRF, ID14-2 · ADSC CCD
Timeline: Collected May 2002, deposited Dec 2002, released Apr 2003 · 11 months from beam to release
Validation: Clashscore 2.4 · Ramachandran outliers 0.0% · rotamer outliers 0.9%
Paper: Reduced Hybrid Cluster Proteins (Hcp) from Desulfovibrio Desulfuricans Atcc 27774 and Desulfovibrio Vulgaris (Hildenborough): X-Ray Structures at High Resolution Using Synchrotron Radiation (J.Biol.Inorg.Chem., 2003) · cited 47 times (OpenAlex)
What came after: 1 later structure of Hydroxylamine reductase in the PDB

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1OA0Reduced hybrid cluster protein from desulfovibrio desulfuricans x-ray structure at 1.25a resolution2003 · 1.25 Å

Protein: Prismane protein (DESULFOVIBRIO DESULFURICANS)
Resolution: 1.25 Å · R_work 0.133, R_free 0.150
Space group: P 1
Cell: a = 57.8, b = 62.0, c = 72.8 Å; α = 82.7, β = 73.7, γ = 87.4°
Size: 118.7 kDa · 1,088 residues in 2 chains · 10,655 atoms
Ligands: MES, SF3, SF4
Data: ESRF, ID14-2 · ADSC CCD
Timeline: Collected Aug 2001, deposited Dec 2002, released Apr 2003 · 20 months from beam to release
Validation: Clashscore 3.1 · Ramachandran outliers 0.0% · rotamer outliers 1.6%
Paper: Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation. (J. Biol. Inorg. Chem., 2003) · cited 47 times (OpenAlex)
What came after: 1 later structure of Hydroxylamine reductase in the PDB

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1GYOCrystal structure of the di-tetraheme cytochrome c3 from Desulfovibrio gigas at 1.2 Angstrom resolution2002 · 1.2 Å · featured

Protein: Cytochrome c3, a dimeric class iii c-type cytochrome (DESULFOVIBRIO GIGAS)
Resolution: 1.2 Å
Space group: P 31
Cell: a = 56.7, b = 56.7, c = 94.2 Å; α = 90.0, β = 90.0, γ = 120.0°
Size: 29.6 kDa · 218 residues in 2 chains · 2,349 atoms
Ligands: GOL, HEC
Data: EMBL Hamburg, BW7B · MARRESEARCH
Timeline: Collected May 1997, deposited Apr 2002, released May 2002 · 5.0 years from beam to release
Validation: Clashscore 2.0 · Ramachandran outliers 0.0% · rotamer outliers 1.1%
Paper: Structure of Dimeric Cytochrome C3 from Desulfovibrio Gigas at 1.2 A Resolution (Acta Crystallogr.,Sect.D, 2003) · cited 25 times (OpenAlex)
What came after: 0 later structures of Cytochrome C3=26 kDa subunit of A dimeric class III C-type cytochrome in the PDB

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Details from the PDB (RCSB and PDBe), citation counts from OpenAlex, refreshed about once a month. "What came after" counts later entries of the same protein (matched by UniProt). The density is the 2mFo–DFc map (and the difference map) from PDBe.