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6giq

Saccharomyces cerevisiae respiratory supercomplex III2IV

Method: ELECTRON MICROSCOPY Dmax: 214.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

BJ4_G0001550.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5Q3X1

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain A； UniProt 1–457 Chain L； UniProt 1–457 Not recorded Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8YHQ Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state Deposited 2024-02-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 27–457（431 aa）
Chain J 27–457（431 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6K methyl ~{N}-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]phenyl]-~{N}-methoxy-carbamate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.42 Å
8YIL Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 27–457（431 aa）
Chain L 27–457（431 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 86T metyltetraprole × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.58 Å
8YIN Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF23694-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 27–457（431 aa）
Chain L 27–457（431 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6O 1-[2-[(4,6-dimethyl-1,3-benzothiazol-2-yl)sulfanylmethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.74 Å
8YIO Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 27–457（431 aa）
Chain L 27–457（431 aa）
Not recorded AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
8ZJC Cryo-EM structure of Saccharomyces cerevisiae bc1 complex Deposited 2024-05-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 27–457（431 aa）
Chain L 27–457（431 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
8ZMT Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state Deposited 2024-05-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain A 27–457（431 aa）
Chain L 27–457（431 aa）
Not recorded A1D6P 1-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.52 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q3X1_YEASX
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–457； UniProt 1–457 Author chain L； PDBConstruct 1–457； UniProt 1–457

Cytochrome b-c1 complex subunit 2, mitochondrial

OrganismNot specified

UniProt A0A6A5Q625

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain B； UniProt 1–368 Chain M； UniProt 1–368 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8YHQ Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state Deposited 2024-02-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain B 17–368（352 aa）
Chain K 17–368（352 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6K methyl ~{N}-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]phenyl]-~{N}-methoxy-carbamate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.42 Å
8YIL Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain B 17–368（352 aa）
Chain M 17–368（352 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 86T metyltetraprole × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.58 Å
8YIN Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF23694-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain B 17–368（352 aa）
Chain M 17–368（352 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6O 1-[2-[(4,6-dimethyl-1,3-benzothiazol-2-yl)sulfanylmethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.74 Å
8YIO Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain B 17–368（352 aa）
Chain M 17–368（352 aa）
Not recorded AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
8ZJC Cryo-EM structure of Saccharomyces cerevisiae bc1 complex Deposited 2024-05-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain B 17–368（352 aa）
Chain M 17–368（352 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
8ZMT Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state Deposited 2024-05-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain B 17–368（352 aa）
Chain M 17–368（352 aa）
Not recorded A1D6P 1-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.52 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q625_YEASX
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–368； UniProt 1–368 Author chain M； PDBConstruct 1–368； UniProt 1–368

Cytochrome b

OrganismNot specified

UniProt A0A0G3F5W7

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain C； UniProt 1–385 Chain N； UniProt 1–385 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8YHQ Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state Deposited 2024-02-28 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain C 1–385（385 aa）
Chain L 1–385（385 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6K methyl ~{N}-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]phenyl]-~{N}-methoxy-carbamate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.42 Å
8YIL Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state Deposited 2024-02-29 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain C 1–385（385 aa）
Chain N 1–385（385 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 86T metyltetraprole × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.58 Å
8YIN Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF23694-bound state Deposited 2024-02-29 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain C 1–385（385 aa）
Chain N 1–385（385 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6O 1-[2-[(4,6-dimethyl-1,3-benzothiazol-2-yl)sulfanylmethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.74 Å
8YIO Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state Deposited 2024-02-29 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain C 1–385（385 aa）
Chain N 1–385（385 aa）
Not recorded AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
8ZJC Cryo-EM structure of Saccharomyces cerevisiae bc1 complex Deposited 2024-05-14 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain C 1–385（385 aa）
Chain N 1–385（385 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
8ZMT Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state Deposited 2024-05-23 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain C 1–385（385 aa）
Chain N 1–385（385 aa）
Not recorded A1D6P 1-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.52 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0G3F5W7_YEASX
Isoform —
PDB entities 3
Chains and sequence ranges Author chain C； PDBConstruct 1–385； UniProt 1–385 Author chain N； PDBConstruct 1–385； UniProt 1–385

BJ4_G0049990.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A5B9RH60

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain D； UniProt 1–309 Chain O； UniProt 1–309 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8YHQ Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state Deposited 2024-02-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain D 62–309（248 aa）
Chain M 62–309（248 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6K methyl ~{N}-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]phenyl]-~{N}-methoxy-carbamate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.42 Å
8YIL Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain D 62–309（248 aa）
Chain O 62–309（248 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 86T metyltetraprole × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.58 Å
8YIN Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF23694-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain D 62–309（248 aa）
Chain O 62–309（248 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6O 1-[2-[(4,6-dimethyl-1,3-benzothiazol-2-yl)sulfanylmethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.74 Å
8YIO Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain D 62–309（248 aa）
Chain O 62–309（248 aa）
Not recorded AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
8ZJC Cryo-EM structure of Saccharomyces cerevisiae bc1 complex Deposited 2024-05-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain D 62–309（248 aa）
Chain O 62–309（248 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
8ZMT Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state Deposited 2024-05-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain D 62–309（248 aa）
Chain O 62–309（248 aa）
Not recorded A1D6P 1-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.52 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5B9RH60_YEASX
Isoform —
PDB entities 4
Chains and sequence ranges Author chain D； PDBConstruct 1–309； UniProt 1–309 Author chain O； PDBConstruct 1–309； UniProt 1–309

Cytochrome b-c1 complex subunit Rieske, mitochondrial

OrganismNot specified

UniProt A0A6A5PX11

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain E； UniProt 1–215 Chain P； UniProt 1–215 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5PX11_YEASX
Isoform —
PDB entities 5
Chains and sequence ranges Author chain E； PDBConstruct 1–215； UniProt 1–215 Author chain P； PDBConstruct 1–215； UniProt 1–215

QCR6 isoform 1

OrganismNot specified

UniProt A0A6A5Q022

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain F； UniProt 1–147 Chain Q； UniProt 1–147 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5Q022_YEASX
Isoform —
PDB entities 6
Chains and sequence ranges Author chain F； PDBConstruct 1–147； UniProt 1–147 Author chain Q； PDBConstruct 1–147； UniProt 1–147

Complex III subunit 7

OrganismNot specified

UniProt A0A6A5Q2H4

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain G； UniProt 1–127 Chain R； UniProt 1–127 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8YHQ Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state Deposited 2024-02-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 2–127（126 aa）
Chain P 2–127（126 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6K methyl ~{N}-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]phenyl]-~{N}-methoxy-carbamate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.42 Å
8YIL Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 2–127（126 aa）
Chain R 2–127（126 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 86T metyltetraprole × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.58 Å
8YIN Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF23694-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 2–127（126 aa）
Chain R 2–127（126 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6O 1-[2-[(4,6-dimethyl-1,3-benzothiazol-2-yl)sulfanylmethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.74 Å
8YIO Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 2–127（126 aa）
Chain R 2–127（126 aa）
Not recorded AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
8ZJC Cryo-EM structure of Saccharomyces cerevisiae bc1 complex Deposited 2024-05-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 2–127（126 aa）
Chain R 2–127（126 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
8ZMT Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state Deposited 2024-05-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain G 2–127（126 aa）
Chain R 2–127（126 aa）
Not recorded A1D6P 1-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.52 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q2H4_YEASX
Isoform —
PDB entities 7
Chains and sequence ranges Author chain G； PDBConstruct 1–127； UniProt 1–127 Author chain R； PDBConstruct 1–127； UniProt 1–127

BJ4_G0028260.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PU80

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain H； UniProt 1–94 Chain S； UniProt 1–94 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8YHQ Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state Deposited 2024-02-28 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 2–94（93 aa）
Chain Q 2–94（93 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6K methyl ~{N}-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]phenyl]-~{N}-methoxy-carbamate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.42 Å
8YIL Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 2–94（93 aa）
Chain S 2–94（93 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 86T metyltetraprole × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.58 Å
8YIN Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF23694-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 2–94（93 aa）
Chain S 2–94（93 aa）
Not recorded 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 A1D6O 1-[2-[(4,6-dimethyl-1,3-benzothiazol-2-yl)sulfanylmethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 2.74 Å
8YIO Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state Deposited 2024-02-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 2–94（93 aa）
Chain S 2–94（93 aa）
Not recorded AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.35 Å
8ZJC Cryo-EM structure of Saccharomyces cerevisiae bc1 complex Deposited 2024-05-14 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 2–94（93 aa）
Chain S 2–94（93 aa）
Not recorded UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS,0.1%DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
8ZMT Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state Deposited 2024-05-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 2–94（93 aa）
Chain S 2–94（93 aa）
Not recorded A1D6P 1-[2-[[1-(4-chlorophenyl)pyrazol-3-yl]oxymethyl]-3-methyl-phenyl]-4-methyl-1,2,3,4-tetrazol-5-one × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；PBS, 0.1% DDM
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.52 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PU80_YEASX
Isoform —
PDB entities 8
Chains and sequence ranges Author chain H； PDBConstruct 1–94； UniProt 1–94 Author chain S； PDBConstruct 1–94； UniProt 1–94

HLJ1_G0021680.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6L0Z0I8

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain I； UniProt 1–66 Chain T； UniProt 1–66 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6L0Z0I8_YEASX
Isoform —
PDB entities 9
Chains and sequence ranges Author chain I； PDBConstruct 1–66； UniProt 1–66 Author chain T； PDBConstruct 1–66； UniProt 1–66

BJ4_G0023510.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6L0ZE60

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain U； UniProt 1–77 Chain V； UniProt 1–77 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6L0ZE60_YEASX
Isoform —
PDB entities 10
Chains and sequence ranges Author chain U； PDBConstruct 1–77； UniProt 1–77 Author chain V； PDBConstruct 1–77； UniProt 1–77

Cytochrome c oxidase subunit 1

OrganismNot specified

UniProt P00401

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain a； UniProt 1–534 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6HU9 III2-IV2 mitochondrial respiratory supercomplex from S. cerevisiae Deposited 2018-10-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 44 PDB declaration: 44-meric
Chain a 1–534（534 aa）
Chain m 1–534（534 aa）
Not recorded PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 28 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 1 CDL CARDIOLIPIN × 8 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 4 ZN ZINC ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE；3 microL of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 sec
Resolution 3.35 Å
6T0B The III2-IV(5B)2 respiratory supercomplex from S. cerevisiae Deposited 2019-10-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 46 PDB declaration: 46-meric
Chain a 1–534（534 aa）
Chain n 1–534（534 aa）
Not recorded CDL CARDIOLIPIN × 8 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 26 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 7 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 2 HEA HEME-A × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE；3 microliter of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 s
Resolution 2.80 Å
6T15 The III2-IV(5B)1 respiratory supercomplex from S. cerevisiae Deposited 2019-10-03 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 33 PDB declaration: 33-meric
Chain a 1–534（534 aa）
Not recorded PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 18 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 CDL CARDIOLIPIN × 7 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE；3 microliter of sample applied to negatively glow discharged grid, blot force -10; blotting time 8.5 s
Resolution 3.29 Å
6YMX CIII2/CIV respiratory supercomplex from Saccharomyces cerevisiae Deposited 2020-04-10 Different construct Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 32 PDB declaration: 32-meric
Chain a 5–534（530 aa）
Not recorded CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 5 ZN ZINC ION × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.17 Å
6YMY Cytochrome c oxidase from Saccharomyces cerevisiae Deposited 2020-04-10 Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain a 5–534（530 aa）
Not recorded CU COPPER (II) ION × 1 HEA HEME-A × 2 PTY PHOSPHATIDYLETHANOLAMINE × 7 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CUA DINUCLEAR COPPER ION × 1 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 3 ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.41 Å
7Z10 Monomeric respiratory complex IV isolated from S. cerevisiae Deposited 2022-02-24 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain a 1–534（534 aa）
Not recorded CU COPPER (II) ION × 1 HEA HEME-A × 2 MG MAGNESIUM ION × 1 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 3 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE；3 microliters of sample applied to negatively glow discharged grig.
Resolution 3.87 Å
8DH6 Cryo-EM structure of Saccharomyces cerevisiae cytochrome c oxidase (Complex IV) extracted in lipid nanodiscs Deposited 2022-06-25 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain a 1–534（534 aa）
Not recorded CA CALCIUM ION × 1 MG MAGNESIUM ION × 1 CU COPPER (II) ION × 2 HEA HEME-A × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 10 ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.94 Å
8E7S III2IV2 respiratory supercomplex from Saccharomyces cerevisiae with 4 bound UQ6 Deposited 2022-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 44 PDB declaration: 44-meric
Chain K 1–534（534 aa）
Chain k 1–534（534 aa）
Not recorded PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 24 FES FE2/S2 (INORGANIC) CLUSTER × 2 CDL CARDIOLIPIN × 10 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 4 HEA HEME-A × 4 CU COPPER (II) ION × 2 CUA DINUCLEAR COPPER ION × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
8EC0 III2IV respiratory supercomplex from Saccharomyces cerevisiae cardiolipin-lacking mutant Deposited 2022-08-31 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 30 PDB declaration: 30-meric
Chain K 1–534（534 aa）
Not recorded PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 15 PGT (1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 7 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9BPB Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae Deposited 2024-05-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 42 PDB declaration: 42-meric
Chain a 1–534（534 aa）
Chain m 1–534（534 aa）
Not recorded CDL CARDIOLIPIN × 8 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 8 PTY PHOSPHATIDYLETHANOLAMINE × 10 HEA HEME-A × 4 CU COPPER (II) ION × 2 CA CALCIUM ION × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 2 MG MAGNESIUM ION × 2 CUA DINUCLEAR COPPER ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；3 uL of sample, 5 s blot time, 30 s hold time, 0 blot force.
Resolution 2.57 Å
9ETZ III2IV respiratory supercomplex from Saccharomyces cerevisiae Deposited 2024-03-27 Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 32 PDB declaration: 32-meric
Chain a 1–534（534 aa）
Not recorded CDL CARDIOLIPIN × 11 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PEF DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE × 26 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 6 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 CU COPPER (II) ION × 1 HEA HEME-A × 2 CA CALCIUM ION × 1 MG MAGNESIUM ION × 1 CUA DINUCLEAR COPPER ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.40 Å

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

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

Cytochrome c oxidase subunit 2

OrganismNot specified

UniProt A0A0H3WI21

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain b； UniProt 1–251 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A0H3WI21_YEASX
Isoform —
PDB entities 12
Chains and sequence ranges Author chain b； PDBConstruct 1–251； UniProt 1–251

Cytochrome c oxidase subunit 3

OrganismNot specified

UniProt A0A0G3F1J2

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain c； UniProt 1–269 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A0G3F1J2_YEASX
Isoform —
PDB entities 13
Chains and sequence ranges Author chain c； PDBConstruct 1–269； UniProt 1–269

BJ4_G0018620.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PV33

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain d； UniProt 1–155 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

Other PDB Difference from Current Entry 6GIQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7CLV Solution structure of mitochondrial Tim23 channel in complex with a signaling peptide Deposited 2020-07-22 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 1–25（25 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；313.75 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR measurement conditions pH 5；313.75 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR sample composition 0.5 mM 2H, 15N Tim23, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 uM 2H, 15N, 13C Tim23_unlabeled_Peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM 15N, 13C Tim23_unlabeled_Peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM 50% 2H, 13C, 15N Tim23_unlabeled_Peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM IVL-selectively_labeled_Tim23_unlabeled_peptide Tim23_unlabeled_Peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM 50%unlabeled/50%labeled_Tim23_unlabeled_peptide Tim23_unlabeled_Peptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 nM 50%unlabeled/50%labeled_Tim23_unlabeled_peptide [15N, 13C]-peptide_unlabeled_Tim23, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PV33_YEASX
Isoform —
PDB entities 14
Chains and sequence ranges Author chain d； PDBConstruct 1–155； UniProt 1–155

BJ4_G0046460.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5Q8F6

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain e； UniProt 1–153 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5Q8F6_YEASX
Isoform —
PDB entities 15
Chains and sequence ranges Author chain e； PDBConstruct 1–153； UniProt 1–153

BJ4_G0024040.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PUE0

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain f； UniProt 1–148 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5PUE0_YEASX
Isoform —
PDB entities 16
Chains and sequence ranges Author chain f； PDBConstruct 1–148； UniProt 1–148

BJ4_G0043230.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PQU1

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain g； UniProt 1–60 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5PQU1_YEASX
Isoform —
PDB entities 17
Chains and sequence ranges Author chain g； PDBConstruct 1–60； UniProt 1–60

BJ4_G0038800.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PRD8

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain h； UniProt 1–78 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5PRD8_YEASX
Isoform —
PDB entities 18
Chains and sequence ranges Author chain h； PDBConstruct 1–78； UniProt 1–78

Cytochrome c oxidase polypeptide VIIA

OrganismNot specified

UniProt A0A6A5Q104

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain i； UniProt 1–59 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5Q104_YEASX
Isoform —
PDB entities 19
Chains and sequence ranges Author chain i； PDBConstruct 1–59； UniProt 1–59

BJ4_G0035470.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PU81

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain j； UniProt 1–83 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） Cytochrome c oxidase subunit × 1 （A0A6A5PWA0） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5PU81_YEASX
Isoform —
PDB entities 20
Chains and sequence ranges Author chain j； PDBConstruct 1–83； UniProt 1–83

Cytochrome c oxidase subunit

OrganismNot specified

UniProt A0A6A5PWA0

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 × 32 PDB declaration: 32-meric（32） Consistent with protein copy count Chain k； UniProt 1–129 Not recorded BJ4_G0001550.mRNA.1.CDS.1 × 2 （A0A6A5Q3X1） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （A0A6A5Q625） Cytochrome b × 2 （A0A0G3F5W7） BJ4_G0049990.mRNA.1.CDS.1 × 2 （A0A5B9RH60） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （A0A6A5PX11） QCR6 isoform 1 × 2 （A0A6A5Q022） Complex III subunit 7 × 2 （A0A6A5Q2H4） BJ4_G0028260.mRNA.1.CDS.1 × 2 （A0A6A5PU80） HLJ1_G0021680.mRNA.1.CDS.1 × 2 （A0A6L0Z0I8） BJ4_G0023510.mRNA.1.CDS.1 × 2 （A0A6L0ZE60） Cytochrome c oxidase subunit 1 × 1 （P00401） Cytochrome c oxidase subunit 2 × 1 （A0A0H3WI21） Cytochrome c oxidase subunit 3 × 1 （A0A0G3F1J2） BJ4_G0018620.mRNA.1.CDS.1 × 1 （A0A6A5PV33） BJ4_G0046460.mRNA.1.CDS.1 × 1 （A0A6A5Q8F6） BJ4_G0024040.mRNA.1.CDS.1 × 1 （A0A6A5PUE0） BJ4_G0043230.mRNA.1.CDS.1 × 1 （A0A6A5PQU1） BJ4_G0038800.mRNA.1.CDS.1 × 1 （A0A6A5PRD8） Cytochrome c oxidase polypeptide VIIA × 1 （A0A6A5Q104） BJ4_G0035470.mRNA.1.CDS.1 × 1 （A0A6A5PU81） Unknown Cox subunit × 1 6PH (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate × 2 HEC HEME C × 6 8PE (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl octadecanoate × 2 CN5 (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-diphosphaoctadec-1-yl pentadecanoate × 1 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 7PH (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PCF 1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE × 2 9PE (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]ethyl octadecanoate × 2 CN3 (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(propanoyloxy)methyl]-4,6,10,12,15-pentaoxa-5,11-diphosphanonadec-1-yl undecanoate × 1 CU COPPER (II) ION × 1 HEA HEME-A × 2 CUA DINUCLEAR COPPER ION × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.23 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A6A5PWA0_YEASX
Isoform —
PDB entities 21
Chains and sequence ranges Author chain k； PDBConstruct 1–129； UniProt 1–129

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 6giq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6giq
Deposition date deposition_date2018-05-15
Structure title titleSaccharomyces cerevisiae respiratory supercomplex III2IV
Keywords keywordsRespiratory chain, supercomplex, bc1 complex, cytochrome c oxidase, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier63.34 Å
Radius of gyration Rg (electron density) rg_electron62.63 Å
Forward intensity I(0) i04865930000.00
Molecular weight molecular_weight624930.0 kDa
Excluded volume excluded_volume795310 ų
Envelope volume envelope_volume1183300 ų
Hydration-shell volume shell_volume153320 ų
Envelope diameter envelope_diameter219.7 Å
Shell Rg shell_rg66.99 Å
Envelope Rg envelope_rg61.46 Å
Shape Rg shape_rg62.65 Å
Total Rg total_rg62.65 Å
Total atoms total_atoms44120
Residues n_residues5470
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax214.1 Å
Rg (real space) rg_real63.19 Å
Rg uncertainty (real space) rg_real_error2.09 Å
I(0) (real space) i0_real4.8660e+09
I(0) uncertainty (real space) i0_real_error1.0970e+08
Rg (reciprocal space) rg_reciprocal63.44 Å
I(0) (reciprocal space) i0_reciprocal4868000000.0000
Solution quality estimate total_estimate0.8732
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.5 Å
Skewness Skewness skewness0.248
Kurtosis Kurtosis kurtosis-0.446
Angular range angular_range— – 0.1250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha480800000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.785
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (35)

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7. Fold Classification (SCOP + CATH) 32 domains

CATH v4.4 (32 domains)

Domain ID domain_id6giqA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqB02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain C
Domain ID domain_id6giqD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id6giqD02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily100 — Cytochrome c1, transmembrane anchor, C-terminal
Domain ID domain_id6giqE01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily270 — Ubiquinol cytochrome reductase, transmembrane domain
Domain ID domain_id6giqE02
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id6giqF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily20 — Ubiquinol-cytochrome C reductase hinge domain
Domain ID domain_id6giqG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily10 — Cytochrome b-c1 complex subunit 7
Domain ID domain_id6giqH00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily210 — Cytochrome b-c1 complex subunit 8
Domain ID domain_id6giqI00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily260 — Cytochrome b-c1 complex subunit 9
Domain ID domain_id6giqL01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqL02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqM01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqM02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id6giqN00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain C
Domain ID domain_id6giqO01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id6giqO02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily100 — Cytochrome c1, transmembrane anchor, C-terminal
Domain ID domain_id6giqP01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily270 — Ubiquinol cytochrome reductase, transmembrane domain
Domain ID domain_id6giqP02
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id6giqQ00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily20 — Ubiquinol-cytochrome C reductase hinge domain
Domain ID domain_id6giqR00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily10 — Cytochrome b-c1 complex subunit 7
Domain ID domain_id6giqS00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily210 — Cytochrome b-c1 complex subunit 8
Domain ID domain_id6giqT00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily260 — Cytochrome b-c1 complex subunit 9
Domain ID domain_id6giqa00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology210 — Cytochrome C Oxidase; Chain A
Homologous superfamily homologous superfamily10 — Cytochrome c oxidase-like, subunit I domain
Domain ID domain_id6giqb01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily90 —
Domain ID domain_id6giqb02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id6giqc01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70 —
Domain ID domain_id6giqc02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily80 — Cytochrome c oxidase, subunit III, four-helix bundle
Domain ID domain_id6giqf00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily40 — Cytochrome c oxidase, subunit Va/VI
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8. Citations (1)

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9. Files and Curves (10)