8p65

Cytochrome bc1 complex (Bos taurus)

Method: ELECTRON MICROSCOPY Dmax: 167.9 Å Quality: GOOD

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

Cytochrome b-c1 complex subunit 1, mitochondrial

OrganismNot specified

UniProt P31800

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain A; UniProt 35–480 Chain N; UniProt 35–480 Not recorded Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

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

Cytochrome b-c1 complex subunit 2, mitochondrial

OrganismNot specified

UniProt P23004

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain B; UniProt 15–453 Chain O; UniProt 15–453 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name QCR2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–439; UniProt 15–453 Author chain O; PDBConstruct 1–439; UniProt 15–453

Cytochrome b

OrganismNot specified

UniProt P00157

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain C; UniProt 1–379 Chain P; UniProt 1–379 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name CYB_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–379; UniProt 1–379 Author chain P; PDBConstruct 1–379; UniProt 1–379

Cytochrome c1, heme protein, mitochondrial

OrganismNot specified

UniProt P00125

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain D; UniProt 85–325 Chain Q; UniProt 85–325 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name CY1_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 85–325 Author chain Q; PDBConstruct 1–241; UniProt 85–325

Cytochrome b-c1 complex subunit Rieske, mitochondrial

OrganismNot specified

UniProt P13272

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain E; UniProt 79–274 Chain I; UniProt 1–54 Chain R; UniProt 79–274 Chain V; UniProt 1–54 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name UCRI_BOVIN
Isoform
PDB entities 5, 9
Chains and sequence ranges Author chain E; PDBConstruct 1–196; UniProt 79–274 Author chain R; PDBConstruct 1–196; UniProt 79–274 Author chain I; PDBConstruct 1–54; UniProt 1–54 Author chain V; PDBConstruct 1–54; UniProt 1–54

Cytochrome b-c1 complex subunit 7

OrganismNot specified

UniProt P00129

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain F; UniProt 1–111 Chain S; UniProt 1–111 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name QCR7_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–111; UniProt 1–111 Author chain S; PDBConstruct 1–111; UniProt 1–111

Cytochrome b-c1 complex subunit 8

OrganismNot specified

UniProt P13271

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain G; UniProt 1–82 Chain T; UniProt 1–82 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name QCR8_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–82; UniProt 1–82 Author chain T; PDBConstruct 1–82; UniProt 1–82

Cytochrome b-c1 complex subunit 6, mitochondrial

OrganismNot specified

UniProt P00126

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain H; UniProt 14–91 Chain U; UniProt 14–91 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name QCR6_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–78; UniProt 14–91 Author chain U; PDBConstruct 1–78; UniProt 14–91

Cytochrome b-c1 complex subunit 9

OrganismNot specified

UniProt P00130

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain J; UniProt 1–64 Chain W; UniProt 1–64 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 10 × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name QCR9_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–64; UniProt 1–64 Author chain W; PDBConstruct 1–64; UniProt 1–64

Cytochrome b-c1 complex subunit 10

OrganismNot specified

UniProt P07552

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain K; UniProt 1–49 Chain X; UniProt 1–49 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P13272) Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot time of 4s with blot force of -3 Resolution 3.00 Å

Other States of the Same Protein in the Database

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

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

View Construct and Data Evidence
UniProt name QCR10_BOVIN
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–49; UniProt 1–49 Author chain X; PDBConstruct 1–49; UniProt 1–49

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 8p65

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p65
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p65
Deposition date deposition_date2023-05-25
Structure title titleCytochrome bc1 complex (Bos taurus)
Keywords keywordsElectron Transport Chain, Complex III, Respiratory Complex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.47
Radius of gyration Rg (electron density) rg_electron54.56
Forward intensity I(0) i03177230000.00
Molecular weight molecular_weight480190.0 kDa
Excluded volume excluded_volume603430 ų
Envelope volume envelope_volume841910 ų
Hydration-shell volume shell_volume125200 ų
Envelope diameter envelope_diameter180.2
Shell Rg shell_rg60.03
Envelope Rg envelope_rg53.32
Shape Rg shape_rg54.56
Total Rg total_rg54.69
Total atoms total_atoms33820
Residues n_residues4278
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax167.9
Rg (real space) rg_real55.33
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real3.1770e+09
I(0) uncertainty (real space) i0_real_error5.7680e+07
Rg (reciprocal space) rg_reciprocal55.57
I(0) (reciprocal space) i0_reciprocal3178000000.0000
Solution quality estimate total_estimate0.8437
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.0
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.558
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha351300000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.062

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)