› 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
Model geometry
Fit model/data
Data not deposited
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
Cytochrome c1, heme protein, mitochondrial Chain: D
Cytochrome b-c1 complex subunit Rieske, mitochondrial Chain: E
Cytochrome b-c1 complex subunit 7 Chain: F
Cytochrome b-c1 complex subunit 8 Chain: G
Cytochrome b-c1 complex subunit 6, mitochondrial Chain: H
Cytochrome b-c1 complex subunit 9 Chain: I
Cytochrome b-c1 complex subunit 9 Chain: J
Cytochrome b-c1 complex subunit 10 Chain: K

Ligands and Environments


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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
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