› 1qcr

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF BOVINE MITOCHONDRIAL CYTOCHROME BC1 COMPLEX, ALPHA CARBON ATOMS ONLY

Released:
DOI: 10.2210/pdb1qcr/pdb
PDB entry 1qcr coloured by chain, front view.
PDB entry 1qcr coloured by chain, side view.
PDB entry 1qcr coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria.
Xia D, Yu CA, Kim H, Xia JZ, Kachurin AM, Zhang L, Yu L, Deisenhofer J
Science 277 60-6 (1997)
PMID: 9204897

Function and Biology Details

Reaction catalysed: 
Quinol + 2 ferricytochrome c(Side 2) = quinone + 2 ferrocytochrome c(Side 2) + 2 H(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero undecamer (preferred)
PDBe Complex ID:
PDB-CPX-132255 (preferred)
Entry contents:
11 distinct polypeptide molecules
Macromolecules (11 distinct):
Cytochrome b-c1 complex subunit 1, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 446 amino acids
Theoretical weight: 49.25 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P31800 (Residues: 35-480; Coverage: 93%)
Gene name: UQCRC1
Sequence domains:
Cytochrome b-c1 complex subunit 2, mitochondrial Chain: B
Molecule details ›
Chain: B
Length: 423 amino acids
Theoretical weight: 45.02 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P23004 (Residues: 31-453; Coverage: 93%)
Gene name: UQCRC2
Sequence domains:
Cytochrome b Chain: C
Molecule details ›
Chain: C
Length: 378 amino acids
Theoretical weight: 42.49 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00157 (Residues: 2-379; Coverage: 100%)
Gene names: COB, CYTB, MT-CYB, MTCYB
Sequence domains:
Cytochrome c1, heme protein, mitochondrial Chain: D
Molecule details ›
Chain: D
Length: 75 amino acids
Theoretical weight: 8.79 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00125 (Residues: 251-325; Coverage: 23%)
Gene name: CYC1
Cytochrome b-c1 complex subunit Rieske, mitochondrial Chain: E
Molecule details ›
Chain: E
Length: 196 amino acids
Theoretical weight: 21.64 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P13272 (Residues: 79-274; Coverage: 72%)
Gene name: UQCRFS1
Sequence domains:
Cytochrome b-c1 complex subunit 7 Chain: F
Molecule details ›
Chain: F
Length: 103 amino acids
Theoretical weight: 12.73 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00129 (Residues: 9-111; Coverage: 93%)
Gene name: UQCRB
Sequence domains: Ubiquinol-cytochrome C reductase complex 14kD subunit
Cytochrome b-c1 complex subunit 8 Chain: G
Molecule details ›
Chain: G
Length: 70 amino acids
Theoretical weight: 8.29 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P13271 (Residues: 2-71; Coverage: 85%)
Gene name: UQCRQ
Sequence domains: UcrQ family
Cytochrome b-c1 complex subunit 6, mitochondrial Chain: H
Molecule details ›
Chain: H
Length: 60 amino acids
Theoretical weight: 7.09 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00126 (Residues: 31-90; Coverage: 66%)
Gene name: UQCRH
Sequence domains: Ubiquinol-cytochrome C reductase hinge protein
Cytochrome b-c1 complex subunit 9 Chain: I
Molecule details ›
Chain: I
Length: 28 amino acids
Theoretical weight: 2.81 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P13272 (Residues: 21-48; Coverage: 10%)
Gene name: UQCRFS1
Sequence domains: Ubiquinol-cytochrome c reductase 8 kDa, N-terminal
Cytochrome b-c1 complex subunit 9 Chain: J
Molecule details ›
Chain: J
Length: 59 amino acids
Theoretical weight: 6.93 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00130 (Residues: 5-63; Coverage: 92%)
Gene name: UQCR10
Sequence domains: Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like
Cytochrome b-c1 complex subunit 10 Chain: K
Molecule details ›
Chain: K
Length: 45 amino acids
Theoretical weight: 5.06 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P07552 (Residues: 1-45; Coverage: 80%)
Gene names: UQCR, UQCR11
Sequence domains: Ubiquinol-cytochrome C reductase complex, 6.4kD protein

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: I4122
Unit cell:
a: 153.5Å b: 153.5Å c: 597.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.3 0.3 0.375

Quick links

Citations

125 review citations

Membrane protein folding and stability: physical principles.
White et al. (1999)
124 more

12 mentions without citation

Bis-histidine-coordinated hemes in four-helix bundles: how the geometry of the bundle controls the axial imidazole plane orientations in transmembrane cytochromes of mitochondrial complexes II and III and related proteins.
Berry et al. (2008)
11 more