6hu9

III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae

Method: ELECTRON MICROSCOPY Dmax: 260.7 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cytochrome b-c1 complex subunit 1, mitochondrial

OrganismNot specified

UniProt P07256

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain A; UniProt 27–457 Chain L; UniProt 27–457 Not recorded Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–431; UniProt 27–457 Author chain L; PDBConstruct 1–431; UniProt 27–457

Cytochrome b-c1 complex subunit 2, mitochondrial

OrganismNot specified

UniProt P07257

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain B; UniProt 17–368 Chain M; UniProt 17–368 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–352; UniProt 17–368 Author chain M; PDBConstruct 1–352; UniProt 17–368

Cytochrome b

OrganismNot specified

UniProt P00163

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain C; UniProt 1–385 Chain N; UniProt 1–385 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–385; UniProt 1–385 Author chain N; PDBConstruct 1–385; UniProt 1–385

Cytochrome c1, heme protein, mitochondrial

OrganismNot specified

UniProt P07143

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain D; UniProt 62–309 Chain O; UniProt 62–309 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY1_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–248; UniProt 62–309 Author chain O; PDBConstruct 1–248; UniProt 62–309

Cytochrome b-c1 complex subunit Rieske, mitochondrial

OrganismNot specified

UniProt P08067

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain E; UniProt 31–215 Chain P; UniProt 31–215 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–185; UniProt 31–215 Author chain P; PDBConstruct 1–185; UniProt 31–215

Cytochrome b-c1 complex subunit 6

OrganismNot specified

UniProt P00127

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain F; UniProt 1–147 Chain Q; UniProt 1–147 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR6_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–147; UniProt 1–147 Author chain Q; PDBConstruct 1–147; UniProt 1–147

Cytochrome b-c1 complex subunit 7

OrganismNot specified

UniProt P00128

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain G; UniProt 1–127 Chain R; UniProt 1–127 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR7_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–127; UniProt 1–127 Author chain R; PDBConstruct 1–127; UniProt 1–127

Cytochrome b-c1 complex subunit 8

OrganismNot specified

UniProt P08525

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain H; UniProt 2–94 Chain S; UniProt 2–94 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

14 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR8_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–93; UniProt 2–94 Author chain S; PDBConstruct 1–93; UniProt 2–94

Cytochrome b-c1 complex subunit 9

OrganismNot specified

UniProt P22289

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain I; UniProt 1–66 Chain T; UniProt 1–66 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR9_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–66; UniProt 1–66 Author chain T; PDBConstruct 1–66; UniProt 1–66

Cytochrome b-c1 complex subunit 10

OrganismNot specified

UniProt P37299

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain J; UniProt 1–77 Chain U; UniProt 1–77 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR10_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–77; UniProt 1–77 Author chain U; PDBConstruct 1–77; UniProt 1–77

Cytochrome c oxidase subunit 1

OrganismNot specified

UniProt P00401

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain a; UniProt 1–534 Chain m; UniProt 1–534 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX1_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain a; PDBConstruct 1–534; UniProt 1–534 Author chain m; PDBConstruct 1–534; UniProt 1–534

Cytochrome c oxidase subunit 2

OrganismNot specified

UniProt P00410

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain b; UniProt 16–251 Chain n; UniProt 16–251 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX2_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain b; PDBConstruct 1–236; UniProt 16–251 Author chain n; PDBConstruct 1–236; UniProt 16–251

Cytochrome c oxidase subunit 3

OrganismNot specified

UniProt P00420

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain c; UniProt 1–269 Chain o; UniProt 1–269 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX3_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain c; PDBConstruct 1–269; UniProt 1–269 Author chain o; PDBConstruct 1–269; UniProt 1–269

Cytochrome c oxidase subunit 4, mitochondrial

OrganismNot specified

UniProt P04037

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain d; UniProt 26–155 Chain p; UniProt 26–155 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

12 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX4_YEAST
Isoform
PDB entities 14
Chains and sequence ranges Author chain d; PDBConstruct 1–130; UniProt 26–155 Author chain p; PDBConstruct 1–130; UniProt 26–155

Cytochrome c oxidase polypeptide 5A, mitochondrial

OrganismNot specified

UniProt P00424

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain e; UniProt 21–153 Chain q; UniProt 21–153 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX5A_YEAST
Isoform
PDB entities 15
Chains and sequence ranges Author chain e; PDBConstruct 1–133; UniProt 21–153 Author chain q; PDBConstruct 1–133; UniProt 21–153

Cytochrome c oxidase subunit 6, mitochondrial

OrganismNot specified

UniProt P00427

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain f; UniProt 41–148 Chain r; UniProt 41–148 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX6_YEAST
Isoform
PDB entities 16
Chains and sequence ranges Author chain f; PDBConstruct 1–108; UniProt 41–148 Author chain r; PDBConstruct 1–108; UniProt 41–148

Cytochrome c oxidase subunit 7

OrganismNot specified

UniProt P10174

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain g; UniProt 2–60 Chain s; UniProt 2–60 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX7_YEAST
Isoform
PDB entities 17
Chains and sequence ranges Author chain g; PDBConstruct 1–59; UniProt 2–60 Author chain s; PDBConstruct 1–59; UniProt 2–60

Cytochrome c oxidase polypeptide VIII, mitochondrial

OrganismNot specified

UniProt P04039

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain h; UniProt 28–74 Chain t; UniProt 28–74 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX8_YEAST
Isoform
PDB entities 18
Chains and sequence ranges Author chain h; PDBConstruct 1–47; UniProt 28–74 Author chain t; PDBConstruct 1–47; UniProt 28–74

Cytochrome c oxidase subunit 7A

OrganismNot specified

UniProt P07255

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain i; UniProt 2–56 Chain u; UniProt 2–56 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX9_YEAST
Isoform
PDB entities 19
Chains and sequence ranges Author chain i; PDBConstruct 1–55; UniProt 2–56 Author chain u; PDBConstruct 1–55; UniProt 2–56

Cytochrome c oxidase subunit 6B

OrganismNot specified

UniProt Q01519

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain j; UniProt 2–83 Chain v; UniProt 2–83 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX12_YEAST
Isoform
PDB entities 20
Chains and sequence ranges Author chain j; PDBConstruct 1–82; UniProt 2–83 Author chain v; PDBConstruct 1–82; UniProt 2–83

Cytochrome c oxidase subunit 6A, mitochondrial

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P32799

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain k; UniProt 10–129 Chain w; UniProt 10–129 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cox26 × 2 (Q2V2P9) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX13_YEAST
Isoform
PDB entities 21
Chains and sequence ranges Author chain k; PDBConstruct 1–120; UniProt 10–129 Author chain w; PDBConstruct 1–120; UniProt 10–129

Cox26

OrganismNot specified

UniProt Q2V2P9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 44 PDB declaration: 44-meric(44) Consistent with protein copy count Chain l; UniProt 1–66 Chain x; UniProt 1–66 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P07256) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P07257) Cytochrome b × 2 (P00163) Cytochrome c1, heme protein, mitochondrial × 2 (P07143) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P08067) Cytochrome b-c1 complex subunit 6 × 2 (P00127) Cytochrome b-c1 complex subunit 7 × 2 (P00128) Cytochrome b-c1 complex subunit 8 × 2 (P08525) Cytochrome b-c1 complex subunit 9 × 2 (P22289) Cytochrome b-c1 complex subunit 10 × 2 (P37299) Cytochrome c oxidase subunit 1 × 2 (P00401) Cytochrome c oxidase subunit 2 × 2 (P00410) Cytochrome c oxidase subunit 3 × 2 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 2 (P04037) Cytochrome c oxidase polypeptide 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7 × 2 (P10174) Cytochrome c oxidase polypeptide VIII, mitochondrial × 2 (P04039) Cytochrome c oxidase subunit 7A × 2 (P07255) Cytochrome c oxidase subunit 6B × 2 (Q01519) Cytochrome c oxidase subunit 6A, mitochondrial × 2 (P32799) PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE;3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec Resolution 3.35 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YD19A_YEAST
Isoform
PDB entities 22
Chains and sequence ranges Author chain l; PDBConstruct 1–66; UniProt 1–66 Author chain x; PDBConstruct 1–66; UniProt 1–66

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6hu9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6hu9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6hu9
Deposition date deposition_date2018-10-05
Structure title titleIII2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae
Keywords keywords;Cytochrome c oxidase Cytochrome bc1 Mitochondria Respiratory chain Supercomplex, OXIDOREDUCTASE, ELECTRON TRANSPORT, OXIDOREDUCTASE-ELECTRON TRANSPORT complex ;; OXIDOREDUCTASE/ELECTRON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier75.58
Radius of gyration Rg (electron density) rg_electron75.74
Forward intensity I(0) i09652770000.00
Molecular weight molecular_weight893100.0 kDa
Excluded volume excluded_volume1139800 ų
Envelope volume envelope_volume1644600 ų
Hydration-shell volume shell_volume184910 ų
Envelope diameter envelope_diameter285.7
Shell Rg shell_rg72.25
Envelope Rg envelope_rg74.66
Shape Rg shape_rg75.77
Total Rg total_rg75.57
Total atoms total_atoms62988
Residues n_residues7636
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax260.7
Rg (real space) rg_real79.04
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real9.6750e+09
I(0) uncertainty (real space) i0_real_error1.8530e+08
Rg (reciprocal space) rg_reciprocal74.40
I(0) (reciprocal space) i0_reciprocal9623000000.0000
Solution quality estimate total_estimate0.8683
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary86.9
Skewness Skewness skewness0.588
Kurtosis Kurtosis kurtosis-0.074
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha1.2590
Highest regularization parameter α highest_alpha859000000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.844; Stabil: 0.874; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.155

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (35)

7. Fold Classification (SCOP + CATH) 42 domains

CATH v4.4 (42 domains)

Domain ID domain_id6hu9A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9B02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain C
Domain ID domain_id6hu9D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id6hu9D02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily100 — Cytochrome c1, transmembrane anchor, C-terminal
Domain ID domain_id6hu9E01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily270 — Ubiquinol cytochrome reductase, transmembrane domain
Domain ID domain_id6hu9E02
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id6hu9F00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily20 — Ubiquinol-cytochrome C reductase hinge domain
Domain ID domain_id6hu9G00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily10 — Cytochrome b-c1 complex subunit 7
Domain ID domain_id6hu9H00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily210 — Cytochrome b-c1 complex subunit 8
Domain ID domain_id6hu9I00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily260 — Cytochrome b-c1 complex subunit 9
Domain ID domain_id6hu9L01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9L02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9M01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9M02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6hu9N00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain C
Domain ID domain_id6hu9O01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id6hu9O02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily100 — Cytochrome c1, transmembrane anchor, C-terminal
Domain ID domain_id6hu9P01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily270 — Ubiquinol cytochrome reductase, transmembrane domain
Domain ID domain_id6hu9P02
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id6hu9Q00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily20 — Ubiquinol-cytochrome C reductase hinge domain
Domain ID domain_id6hu9R00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily10 — Cytochrome b-c1 complex subunit 7
Domain ID domain_id6hu9S00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily210 — Cytochrome b-c1 complex subunit 8
Domain ID domain_id6hu9T00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily260 — Cytochrome b-c1 complex subunit 9
Domain ID domain_id6hu9a00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology210 — Cytochrome C Oxidase; Chain A
Homologous superfamily homologous superfamily10 — Cytochrome c oxidase-like, subunit I domain
Domain ID domain_id6hu9b01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily90
Domain ID domain_id6hu9b02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id6hu9c01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id6hu9c02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily80 — Cytochrome c oxidase, subunit III, four-helix bundle
Domain ID domain_id6hu9f00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily40 — Cytochrome c oxidase, subunit Va/VI
Domain ID domain_id6hu9h00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology49 — Cytochrome C Oxidase; Chain L
Homologous superfamily homologous superfamily10 — Cytochrome c oxidase subunit VIIc
Domain ID domain_id6hu9j00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily140 — Cytochrome c oxidase, subunit VIb
Domain ID domain_id6hu9m00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology210 — Cytochrome C Oxidase; Chain A
Homologous superfamily homologous superfamily10 — Cytochrome c oxidase-like, subunit I domain
Domain ID domain_id6hu9n01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily90
Domain ID domain_id6hu9n02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id6hu9o01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id6hu9o02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily80 — Cytochrome c oxidase, subunit III, four-helix bundle
Domain ID domain_id6hu9r00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily40 — Cytochrome c oxidase, subunit Va/VI
Domain ID domain_id6hu9t00
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology49 — Cytochrome C Oxidase; Chain L
Homologous superfamily homologous superfamily10 — Cytochrome c oxidase subunit VIIc
Domain ID domain_id6hu9v00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily140 — Cytochrome c oxidase, subunit VIb

8. Citations (1)

9. Files and Curves (10)