9w2y

Cryo-EM structure of complex III on the bovine heart submitochondrial particles, III-2

Method: ELECTRON MICROSCOPY Dmax: 180.4 Å Quality: GOOD

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

Cytochrome b-c1 complex subunit 1, mitochondrial

Bos taurus

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 L; 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 Resolution 2.40 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 L; PDBConstruct 1–446; UniProt 35–480

Cytochrome b-c1 complex subunit 2, mitochondrial

Bos taurus

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 29–453 Chain M; UniProt 29–453 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 Resolution 2.40 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 1–425; UniProt 29–453 Author chain M; PDBConstruct 1–425; UniProt 29–453

Cytochrome b

Bos taurus

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 2–379 Chain N; UniProt 2–379 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 Resolution 2.40 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 1–378; UniProt 2–379 Author chain N; PDBConstruct 1–378; UniProt 2–379

Cytochrome c1, heme protein, mitochondrial

Bos taurus

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 O; 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 Resolution 2.40 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 O; PDBConstruct 1–241; UniProt 85–325

Cytochrome b-c1 complex subunit Rieske, mitochondrial

Bos taurus

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 1–57 Chain P; UniProt 79–274 Chain T; UniProt 1–57 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 Resolution 2.40 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 P; PDBConstruct 1–196; UniProt 79–274 Author chain I; PDBConstruct 1–57; UniProt 1–57 Author chain T; PDBConstruct 1–57; UniProt 1–57

Cytochrome b-c1 complex subunit 7

Bos taurus

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 7–111 Chain Q; UniProt 7–111 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 Resolution 2.40 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 1–105; UniProt 7–111 Author chain Q; PDBConstruct 1–105; UniProt 7–111

Cytochrome b-c1 complex subunit 8

Bos taurus

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 2–76 Chain R; UniProt 2–76 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 Resolution 2.40 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 1–75; UniProt 2–76 Author chain R; PDBConstruct 1–75; UniProt 2–76

Cytochrome b-c1 complex subunit 6, mitochondrial

Bos taurus

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 25–91 Chain S; UniProt 25–91 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 Resolution 2.40 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 1–67; UniProt 25–91 Author chain S; PDBConstruct 1–67; UniProt 25–91

Cytochrome b-c1 complex subunit 9

Bos taurus

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 2–62 Chain U; UniProt 2–62 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 Resolution 2.40 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 1–61; UniProt 2–62 Author chain U; PDBConstruct 1–61; UniProt 2–62

Cytochrome b-c1 complex subunit 10

Bos taurus

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 2–53 Chain V; UniProt 2–53 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 Resolution 2.40 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 1–52; UniProt 2–53 Author chain V; PDBConstruct 1–52; UniProt 2–53

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 9w2y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9w2y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9w2y
Deposition date deposition_date2025-07-28
Structure title titleCryo-EM structure of complex III on the bovine heart submitochondrial particles, III-2
Keywords keywordsrespiratory chain complex, supercomplex, submitochondrial particles, MOTOR PROTEIN, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.77
Radius of gyration Rg (electron density) rg_electron55.89
Forward intensity I(0) i03066710000.00
Molecular weight molecular_weight472200.0 kDa
Excluded volume excluded_volume593700 ų
Envelope volume envelope_volume892450 ų
Hydration-shell volume shell_volume130020 ų
Envelope diameter envelope_diameter178.9
Shell Rg shell_rg61.09
Envelope Rg envelope_rg54.34
Shape Rg shape_rg55.88
Total Rg total_rg56.07
Total atoms total_atoms33266
Residues n_residues4206
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 dmax180.4
Rg (real space) rg_real56.61
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real3.0670e+09
I(0) uncertainty (real space) i0_real_error5.9830e+07
Rg (reciprocal space) rg_reciprocal56.87
I(0) (reciprocal space) i0_reciprocal3068000000.0000
Solution quality estimate total_estimate0.8696
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.4
Skewness Skewness skewness0.215
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha438900000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.517

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)