9bpb

Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae

Method: ELECTRON MICROSCOPY Dmax: 209.6 Å Quality: EXCELLENT

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain A; UniProt 1–457 Chain K; UniProt 1–457 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–457; UniProt 1–457 Author chain K; PDBConstruct 1–457; UniProt 1–457

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain B; UniProt 1–368 Chain L; UniProt 1–368 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–368; UniProt 1–368 Author chain L; PDBConstruct 1–368; UniProt 1–368

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain C; UniProt 1–385 Chain M; 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 M; 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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain D; UniProt 1–309 Chain N; UniProt 1–309 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–309; UniProt 1–309 Author chain N; PDBConstruct 1–309; UniProt 1–309

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain E; UniProt 1–215 Chain O; UniProt 1–215 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–215; UniProt 1–215 Author chain O; PDBConstruct 1–215; UniProt 1–215

Cytochrome b-c1 complex subunit 6, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain F; UniProt 1–147 Chain P; 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, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 P; PDBConstruct 1–147; UniProt 1–147

Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial

Saccharomyces cerevisiae W303

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain G; UniProt 1–127 Chain Q; 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 Q; PDBConstruct 1–127; UniProt 1–127

Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial

Saccharomyces cerevisiae W303

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain G; UniProt 27–78 Chain Q; UniProt 27–78 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 7
Chains and sequence ranges Author chain G; PDBConstruct 132–183; UniProt 27–78 Author chain Q; PDBConstruct 132–183; UniProt 27–78

Cytochrome b-c1 complex subunit 8, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain H; UniProt 1–94 Chain R; UniProt 1–94 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–94; UniProt 1–94 Author chain R; PDBConstruct 1–94; UniProt 1–94

Cytochrome b-c1 complex subunit 9, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain I; UniProt 1–66 Chain S; 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 S; PDBConstruct 1–66; UniProt 1–66

Cytochrome b-c1 complex subunit 10, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain J; UniProt 1–77 Chain T; 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 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 subunit 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 T; 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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 subunit 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain b; UniProt 1–251 Chain n; UniProt 1–251 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 subunit 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–251; UniProt 1–251 Author chain n; PDBConstruct 1–251; UniProt 1–251

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 subunit 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain d; UniProt 1–155 Chain p; UniProt 1–155 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–155; UniProt 1–155 Author chain p; PDBConstruct 1–155; UniProt 1–155

Cytochrome c oxidase subunit 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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain e; UniProt 1–153 Chain q; UniProt 1–153 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–153; UniProt 1–153 Author chain q; PDBConstruct 1–153; UniProt 1–153

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain f; UniProt 1–148 Chain r; UniProt 1–148 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–148; UniProt 1–148 Author chain r; PDBConstruct 1–148; UniProt 1–148

Cytochrome c oxidase subunit 7, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain g; UniProt 1–60 Chain s; UniProt 1–60 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 1–60; UniProt 1–60 Author chain s; PDBConstruct 1–60; UniProt 1–60

Cytochrome c oxidase subunit 9, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain i; UniProt 1–59 Chain u; UniProt 1–59 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 18
Chains and sequence ranges Author chain i; PDBConstruct 1–59; UniProt 1–59 Author chain u; PDBConstruct 1–59; UniProt 1–59

Cytochrome c oxidase subunit 12, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain j; UniProt 1–83 Chain v; UniProt 1–83 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 19
Chains and sequence ranges Author chain j; PDBConstruct 1–83; UniProt 1–83 Author chain v; PDBConstruct 1–83; UniProt 1–83

Cytochrome c oxidase subunit 13, mitochondrial

OrganismNot specified

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain k; UniProt 1–129 Chain w; UniProt 1–129 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 26, mitochondrial × 2 (Q2V2P9) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 20
Chains and sequence ranges Author chain k; PDBConstruct 1–129; UniProt 1–129 Author chain w; PDBConstruct 1–129; UniProt 1–129

Cytochrome c oxidase subunit 26, mitochondrial

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 Insufficient information Heteromer Protein × 42 PDB declaration: 42-meric(42) 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, mitochondrial × 2 (P00127) Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial × 2 (P00128,P04039) Cytochrome b-c1 complex subunit 8, mitochondrial × 2 (P08525) Cytochrome b-c1 complex subunit 9, mitochondrial × 2 (P22289) Cytochrome b-c1 complex subunit 10, mitochondrial × 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 5A, mitochondrial × 2 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 2 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 2 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 2 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 2 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 2 (P32799) CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 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 × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force. Resolution 2.57 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 COX26_YEAST
Isoform
PDB entities 21
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 9bpb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bpb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bpb
Deposition date deposition_date2024-05-07
Structure title titleTethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae
Keywords keywordsComplex, Oxidoreductase, Respiration, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier77.38
Radius of gyration Rg (electron density) rg_electron77.72
Forward intensity I(0) i09069100000.00
Molecular weight molecular_weight862440.0 kDa
Excluded volume excluded_volume1099300 ų
Envelope volume envelope_volume1697400 ų
Hydration-shell volume shell_volume187570 ų
Envelope diameter envelope_diameter295.3
Shell Rg shell_rg73.05
Envelope Rg envelope_rg76.29
Shape Rg shape_rg77.76
Total Rg total_rg77.53
Total atoms total_atoms61288
Residues n_residues7384
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 dmax209.6
Rg (real space) rg_real73.01
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real8.7050e+09
I(0) uncertainty (real space) i0_real_error1.6190e+08
Rg (reciprocal space) rg_reciprocal76.02
I(0) (reciprocal space) i0_reciprocal9036000000.0000
Solution quality estimate total_estimate0.9242
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary83.9
Skewness Skewness skewness0.335
Kurtosis Kurtosis kurtosis-0.399
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.3209
Highest regularization parameter α highest_alpha696600000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.983; Stabil: 0.986; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.136

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (40)

8. Citations (1)

9. Files and Curves (10)