6ymy

Cytochrome c oxidase from Saccharomyces cerevisiae

Method: ELECTRON MICROSCOPY Dmax: 126.8 Å Quality: GOOD

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

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain a; UniProt 5–534 Not recorded Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 1
Chains and sequence ranges Author chain a; PDBConstruct 1–530; UniProt 5–534

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain b; UniProt 16–251 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 2
Chains and sequence ranges Author chain b; 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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain c; UniProt 2–269 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 3
Chains and sequence ranges Author chain c; PDBConstruct 1–268; UniProt 2–269

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain d; UniProt 30–146 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 4
Chains and sequence ranges Author chain d; PDBConstruct 1–117; UniProt 30–146

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 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain e; UniProt 25–152 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 5
Chains and sequence ranges Author chain e; PDBConstruct 1–128; UniProt 25–152

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain f; UniProt 47–145 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 6
Chains and sequence ranges Author chain f; PDBConstruct 1–99; UniProt 47–145

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 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain g; UniProt 3–57 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 7
Chains and sequence ranges Author chain g; PDBConstruct 1–55; UniProt 3–57

Cytochrome c oxidase subunit 8, 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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain h; UniProt 28–78 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 8
Chains and sequence ranges Author chain h; PDBConstruct 1–51; UniProt 28–78

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 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain i; UniProt 2–53 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 9
Chains and sequence ranges Author chain i; PDBConstruct 1–52; UniProt 2–53

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 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain j; UniProt 6–83 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 10
Chains and sequence ranges Author chain j; PDBConstruct 1–78; UniProt 6–83

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 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain k; UniProt 16–129 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 26, mitochondrial × 1 (Q2V2P9) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 11
Chains and sequence ranges Author chain k; PDBConstruct 1–114; UniProt 16–129

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 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain m; UniProt 26–63 Not recorded Cytochrome c oxidase subunit 1 × 1 (P00401) Cytochrome c oxidase subunit 2 × 1 (P00410) Cytochrome c oxidase subunit 3 × 1 (P00420) Cytochrome c oxidase subunit 4, mitochondrial × 1 (P04037) Cytochrome c oxidase subunit 5A, mitochondrial × 1 (P00424) Cytochrome c oxidase subunit 6, mitochondrial × 1 (P00427) Cytochrome c oxidase subunit 7, mitochondrial × 1 (P10174) Cytochrome c oxidase subunit 8, mitochondrial × 1 (P04039) Cytochrome c oxidase subunit 9, mitochondrial × 1 (P07255) Cytochrome c oxidase subunit 12, mitochondrial × 1 (Q01519) Cytochrome c oxidase subunit 13, mitochondrial × 1 (P32799) CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 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 × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 12
Chains and sequence ranges Author chain m; PDBConstruct 1–38; UniProt 26–63

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 6ymy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ymy
Deposition date deposition_date2020-04-10
Structure title titleCytochrome c oxidase from Saccharomyces cerevisiae
Keywords keywordsCIV, CytcO, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.68
Radius of gyration Rg (electron density) rg_electron38.37
Forward intensity I(0) i0540863000.00
Molecular weight molecular_weight207050.0 kDa
Excluded volume excluded_volume265470 ų
Envelope volume envelope_volume332180 ų
Hydration-shell volume shell_volume68903 ų
Envelope diameter envelope_diameter136.6
Shell Rg shell_rg46.39
Envelope Rg envelope_rg38.81
Shape Rg shape_rg38.37
Total Rg total_rg38.86
Total atoms total_atoms14612
Residues n_residues1766
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 dmax126.8
Rg (real space) rg_real39.56
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real5.4090e+08
I(0) uncertainty (real space) i0_real_error8.6670e+06
Rg (reciprocal space) rg_reciprocal39.64
I(0) (reciprocal space) i0_reciprocal540900000.0000
Solution quality estimate total_estimate0.8917
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.4
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha118500000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.821

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6ymya01
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_id6ymyb01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins

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9. Files and Curves (10)