2ybb

Fitted model for bovine mitochondrial supercomplex I1III2IV1 by single particle cryo-EM (EMD-1876)

Method: ELECTRON MICROSCOPY Dmax: 259.1 Å Quality: EXCELLENT

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

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1

OrganismNot specified

UniProt Q56222

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 1; UniProt 1–438 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO1_THET8
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–438; UniProt 1–438

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2

OrganismNot specified

UniProt Q56221

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 2; UniProt 1–181 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO2_THET8
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–181; UniProt 1–181

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3

OrganismNot specified

UniProt Q56223

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 3; UniProt 1–783 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO3_THET8
Isoform
PDB entities 3
Chains and sequence ranges Author chain 3; PDBConstruct 1–783; UniProt 1–783

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4

OrganismNot specified

UniProt Q56220

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 4; UniProt 1–409 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO4_THET8
Isoform
PDB entities 4
Chains and sequence ranges Author chain 4; PDBConstruct 1–409; UniProt 1–409

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5

OrganismNot specified

UniProt Q56219

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 5; UniProt 1–207 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

18 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO5_THET8
Isoform
PDB entities 5
Chains and sequence ranges Author chain 5; PDBConstruct 1–207; UniProt 1–207

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6

OrganismNot specified

UniProt Q56218

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 6; UniProt 1–181 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO6_THET8
Isoform
PDB entities 6
Chains and sequence ranges Author chain 6; PDBConstruct 1–181; UniProt 1–181

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15

OrganismNot specified

UniProt Q5SKZ7

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 7; UniProt 1–129 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO15_THET8
Isoform
PDB entities 7
Chains and sequence ranges Author chain 7; PDBConstruct 1–129; UniProt 1–129

NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9

OrganismNot specified

UniProt Q56224

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain 8; UniProt 1–182 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO9_THET8
Isoform
PDB entities 8
Chains and sequence ranges Author chain 8; PDBConstruct 1–182; UniProt 1–182

CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL

OrganismNot specified

UniProt P31800

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain A; UniProt 35–480 Chain a; UniProt 35–480 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR1_BOVIN
Isoform
PDB entities 9
Chains and sequence ranges Author chain A; PDBConstruct 1–446; UniProt 35–480 Author chain a; PDBConstruct 1–446; UniProt 35–480

CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL

OrganismNot specified

UniProt P23004

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain B; UniProt 15–453 Chain b; UniProt 15–453 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR2_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain B; PDBConstruct 1–439; UniProt 15–453 Author chain b; PDBConstruct 1–439; UniProt 15–453

CYTOCHROME B

OrganismNot specified

UniProt P00157

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain C; UniProt 1–379 Chain c; UniProt 1–379 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

45 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB_BOVIN
Isoform
PDB entities 11
Chains and sequence ranges Author chain C; PDBConstruct 1–379; UniProt 1–379 Author chain c; PDBConstruct 1–379; UniProt 1–379

CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL

OrganismNot specified

UniProt P00125

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain D; UniProt 85–325 Chain d; UniProt 85–325 Fragment:RESIDUES 85-325 NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY1_BOVIN
Isoform
PDB entities 12
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 85–325 Author chain d; PDBConstruct 1–241; UniProt 85–325

CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL

OrganismNot specified

UniProt P13272

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain E; UniProt 79–274 Chain I; UniProt 14–78 Chain e; UniProt 79–274 Chain i; UniProt 14–78 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

48 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_BOVIN
Isoform
PDB entities 13, 17
Chains and sequence ranges Author chain E; PDBConstruct 1–196; UniProt 79–274 Author chain e; PDBConstruct 1–196; UniProt 79–274 Author chain I; PDBConstruct 1–65; UniProt 14–78 Author chain i; PDBConstruct 1–65; UniProt 14–78

CYTOCHROME B-C1 COMPLEX SUBUNIT 7

OrganismNot specified

UniProt P00129

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain F; UniProt 2–111 Chain f; UniProt 2–111 Mutation:YES NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

45 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR7_BOVIN
Isoform
PDB entities 14
Chains and sequence ranges Author chain F; PDBConstruct 1–110; UniProt 2–111 Author chain f; PDBConstruct 1–110; UniProt 2–111

CYTOCHROME B-C1 COMPLEX SUBUNIT 8

OrganismNot specified

UniProt P13271

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain G; UniProt 2–82 Chain g; UniProt 2–82 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR8_BOVIN
Isoform
PDB entities 15
Chains and sequence ranges Author chain G; PDBConstruct 1–81; UniProt 2–82 Author chain g; PDBConstruct 1–81; UniProt 2–82

CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL

OrganismNot specified

UniProt P00126

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain H; UniProt 14–91 Chain h; UniProt 14–91 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR6_BOVIN
Isoform
PDB entities 16
Chains and sequence ranges Author chain H; PDBConstruct 1–78; UniProt 14–91 Author chain h; PDBConstruct 1–78; UniProt 14–91

CYTOCHROME B-C1 COMPLEX SUBUNIT 9

OrganismNot specified

UniProt P00130

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain J; UniProt 2–63 Chain j; UniProt 2–63 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR9_BOVIN
Isoform
PDB entities 18
Chains and sequence ranges Author chain J; PDBConstruct 1–62; UniProt 2–63 Author chain j; PDBConstruct 1–62; UniProt 2–63

CYTOCHROME B-C1 COMPLEX SUBUNIT 10

OrganismNot specified

UniProt P07552

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain K; UniProt 1–56 Chain k; UniProt 1–56 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

29 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR10_BOVIN
Isoform
PDB entities 19
Chains and sequence ranges Author chain K; PDBConstruct 1–56; UniProt 1–56 Author chain k; PDBConstruct 1–56; UniProt 1–56

CYTOCHROME C OXIDASE SUBUNIT 1

OrganismNot specified

UniProt P00396

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain L; UniProt 1–514 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX1_BOVIN
Isoform
PDB entities 20
Chains and sequence ranges Author chain L; PDBConstruct 1–514; UniProt 1–514

CYTOCHROME C OXIDASE SUBUNIT 2

OrganismNot specified

UniProt P68530

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain M; UniProt 1–227 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

88 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX2_BOVIN
Isoform
PDB entities 21
Chains and sequence ranges Author chain M; PDBConstruct 1–227; UniProt 1–227

CYTOCHROME C OXIDASE SUBUNIT 3

OrganismNot specified

UniProt P00415

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain N; UniProt 1–261 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

90 other PDB entries and 132 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX3_BOVIN
Isoform
PDB entities 22
Chains and sequence ranges Author chain N; PDBConstruct 1–261; UniProt 1–261

CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL

OrganismNot specified

UniProt P00423

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain O; UniProt 23–169 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX41_BOVIN
Isoform
PDB entities 23
Chains and sequence ranges Author chain O; PDBConstruct 1–147; UniProt 23–169

CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL

OrganismNot specified

UniProt P00426

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain P; UniProt 44–152 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX5A_BOVIN
Isoform
PDB entities 24
Chains and sequence ranges Author chain P; PDBConstruct 1–109; UniProt 44–152

CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL

OrganismNot specified

UniProt P00428

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain Q; UniProt 32–129 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX5B_BOVIN
Isoform
PDB entities 25
Chains and sequence ranges Author chain Q; PDBConstruct 1–98; UniProt 32–129

CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB

OrganismNot specified

UniProt P07471

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain R; UniProt 13–96 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CX6A2_BOVIN
Isoform
PDB entities 26
Chains and sequence ranges Author chain R; PDBConstruct 1–84; UniProt 13–96

CYTOCHROME C OXIDASE SUBUNIT 6B1

OrganismNot specified

UniProt P00429

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain S; UniProt 2–86 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CX6B1_BOVIN
Isoform
PDB entities 27
Chains and sequence ranges Author chain S; PDBConstruct 1–85; UniProt 2–86

CYTOCHROME C OXIDASE SUBUNIT 6C

OrganismNot specified

UniProt P04038

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain T; UniProt 2–74 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX6C_BOVIN
Isoform
PDB entities 28
Chains and sequence ranges Author chain T; PDBConstruct 1–73; UniProt 2–74

CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL

OrganismNot specified

UniProt P07470

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain U; UniProt 22–80 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CX7A1_BOVIN
Isoform
PDB entities 29
Chains and sequence ranges Author chain U; PDBConstruct 1–59; UniProt 22–80

CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL

OrganismNot specified

UniProt P13183

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain V; UniProt 25–80 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX7B_BOVIN
Isoform
PDB entities 30
Chains and sequence ranges Author chain V; PDBConstruct 1–56; UniProt 25–80

CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL

OrganismNot specified

UniProt P00430

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain W; UniProt 17–63 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

91 other PDB entries and 133 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX7C_BOVIN
Isoform
PDB entities 31
Chains and sequence ranges Author chain W; PDBConstruct 1–47; UniProt 17–63

CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL

OrganismNot specified

UniProt P10175

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain X; UniProt 25–70 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C × 1 (P62894) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

90 other PDB entries and 132 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name COX8B_BOVIN
Isoform
PDB entities 32
Chains and sequence ranges Author chain X; PDBConstruct 1–46; UniProt 25–70

CYTOCHROME C

OrganismNot specified

UniProt P62894

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 × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain Y; UniProt 2–105 Not recorded NADH-QUINONE OXIDOREDUCTASE SUBUNIT 1 × 1 (Q56222) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 2 × 1 (Q56221) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 3 × 1 (Q56223) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 4 × 1 (Q56220) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 5 × 1 (Q56219) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 6 × 1 (Q56218) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 15 × 1 (Q5SKZ7) NADH-QUINONE OXIDOREDUCTASE SUBUNIT 9 × 1 (Q56224) CYTOCHROME B-C1 COMPLEX SUBUNIT 1, MITOCHONDRIAL × 2 (P31800) CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL × 2 (P23004) CYTOCHROME B × 2 (P00157) CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL × 2 (P00125) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 7 × 2 (P00129) CYTOCHROME B-C1 COMPLEX SUBUNIT 8 × 2 (P13271) CYTOCHROME B-C1 COMPLEX SUBUNIT 6, MITOCHONDRIAL × 2 (P00126) CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 (P13272) CYTOCHROME B-C1 COMPLEX SUBUNIT 9 × 2 (P00130) CYTOCHROME B-C1 COMPLEX SUBUNIT 10 × 2 (P07552) CYTOCHROME C OXIDASE SUBUNIT 1 × 1 (P00396) CYTOCHROME C OXIDASE SUBUNIT 2 × 1 (P68530) CYTOCHROME C OXIDASE SUBUNIT 3 × 1 (P00415) CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1, MITOCHONDRIAL × 1 (P00423) CYTOCHROME C OXIDASE SUBUNIT 5A, MITOCHONDRIAL × 1 (P00426) CYTOCHROME C OXIDASE SUBUNIT 5B, MITOCHONDRIAL × 1 (P00428) CYTOCHROME C OXIDASE POLYPEPTIDE VIA, CYTOCHROME C OXIDASE POLYPEPTIDE VB × 1 (P07471) CYTOCHROME C OXIDASE SUBUNIT 6B1 × 1 (P00429) CYTOCHROME C OXIDASE SUBUNIT 6C × 1 (P04038) CYTOCHROME C OXIDASE SUBUNIT 7A1, MITOCHONDRIAL × 1 (P07470) CYTOCHROME C OXIDASE SUBUNIT 7B, MITOCHONDRIAL × 1 (P13183) CYTOCHROME C OXIDASE SUBUNIT 7C, MITOCHONDRIAL × 1 (P00430) CYTOCHROME C OXIDASE SUBUNIT 8B, MITOCHONDRIAL × 1 (P10175) NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT L, × 1 NADH\: UBIQUINONE OXIDOREDUCTASE, MEMBRANE SUBUNIT M, × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT N × 1 NADH-QUINONE OXIDOREDUCTASE SUBUNIT K × 1 SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE × 1 MG MAGNESIUM ION × 7 FES FE2/S2 (INORGANIC) CLUSTER × 4 CA CALCIUM ION × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 5 SMA STIGMATELLIN A × 2 UQ1 UBIQUINONE-1 × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 HEA HEME-A × 2 CU COPPER (II) ION × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE;pH 7.7;10 MM KCL, 15 MM HEPES, RESIDUAL TREHALOSE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 70, TEMPERATURE- 95, INSTRUMENT- CUSTOM-MADE HAND PLUNGER, METHOD- ONE- SIDED BLOTTING FOR 26 - 30 SECONDS BEFORE PLUNGING, DETAILS- SAMPLE WAS ADSORBED TO CARBON FILM FOR 30 SECONDS BEFORE BLOTTING Resolution 19.00 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYC_BOVIN
Isoform
PDB entities 33
Chains and sequence ranges Author chain Y; PDBConstruct 1–104; UniProt 2–105

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 2ybb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2ybb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2ybb
Deposition date deposition_date2011-03-02
Structure title titleFitted model for bovine mitochondrial supercomplex I1III2IV1 by single particle cryo-EM (EMD-1876)
Keywords keywordsSUPERCOMPLEX B, MITOCHONDRIA, RESPIRATORY CHAIN, OXIDOREDUCTASE, AMPHIPOL A8-35, RANDOM CONICAL TILT; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier96.08
Radius of gyration Rg (electron density) rg_electron96.70
Forward intensity I(0) i013804600000.00
Molecular weight molecular_weight1006100.0 kDa
Excluded volume excluded_volume1258600 ų
Envelope volume envelope_volume2285800 ų
Hydration-shell volume shell_volume211350 ų
Envelope diameter envelope_diameter337.3
Shell Rg shell_rg83.40
Envelope Rg envelope_rg90.50
Shape Rg shape_rg96.67
Total Rg total_rg96.71
Total atoms total_atoms70962
Residues n_residues9849
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 dmax259.1
Rg (real space) rg_real91.86
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real1.3270e+10
I(0) uncertainty (real space) i0_real_error2.7730e+08
Rg (reciprocal space) rg_reciprocal92.98
I(0) (reciprocal space) i0_reciprocal13660000000.0000
Solution quality estimate total_estimate0.9178
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary113.4
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.629
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.7374
Highest regularization parameter α highest_alpha243200000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 1.000; Stabil: 0.977; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (52)

8. Citations (2)

9. Files and Curves (10)