› 3bcc

X-ray diffraction
3.7Å resolution

STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN

Released:
DOI: 10.2210/pdb3bcc/pdb
Model geometry
Fit model/data
PDB entry 3bcc coloured by chain, front view.
PDB entry 3bcc coloured by chain, side view.
PDB entry 3bcc coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Electron transfer by domain movement in cytochrome bc1.
Zhang Z, Huang L, Shulmeister VM, Chi YI, Kim KK, Hung LW, Crofts AR, Berry EA, Kim SH
Nature 392 677-84 (1998)
PMID: 9565029

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 icosamer (preferred)
PDBe Complex ID:
PDB-CPX-132268 (preferred)
Entry contents:
10 distinct polypeptide molecules
Macromolecules (10 distinct):
Cytochrome b-c1 complex subunit 1, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 446 amino acids
Theoretical weight: 49.8 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P31800 (Residues: 35-480; Coverage: 93%)
Gene name: UQCRC1
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
Cytochrome b-c1 complex subunit 2, mitochondrial Chain: B
Molecule details ›
Chain: B
Length: 422 amino acids
Theoretical weight: 45.09 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P23004 (Residues: 32-453; Coverage: 93%)
Gene name: UQCRC2
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
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
UBIQUINOL CYTOCHROME C OXIDOREDUCTASE Chain: I
Cytochrome b-c1 complex subunit 9 Chain: J

Ligands and Environments


Cofactor: Ligand HEM 3 x HEM
3 bound ligands:
Ligand SIG 1 x SIG
Ligand AMY 1 x AMY
Ligand FES 1 x FES
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 173.18Å b: 179.73Å c: 238.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.289 0.289 0.321

Quick links

Citations

121 review citations

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

18 mentions without citation

Structural analysis of cytochrome bc1 complexes: implications to the mechanism of function.
Xia et al. (2013)
17 more