› 1gm4

X-ray diffraction
2.05Å resolution

OXIDISED STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS ATCC 27774 at pH 7.6

Released:
DOI: 10.2210/pdb1gm4/pdb
PDB entry 1gm4 coloured by chain, front view.
PDB entry 1gm4 coloured by chain, side view.
PDB entry 1gm4 coloured by chain, top view.
Source organism: Desulfovibrio desulfuricans
Primary publication:
Conformational component in the coupled transfer of multiple electrons and protons in a monomeric tetraheme cytochrome.
Louro RO, Bento I, Matias PM, Catarino T, Baptista AM, Soares CM, Carrondo MA, Turner DL, Xavier AV
J Biol Chem 276 44044-51 (2001)
PMID: 11551953

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192227 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Class III cytochrome C domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.62 KDa
Source organism: Desulfovibrio desulfuricans
UniProt:
  • Canonical: Q9L915 (Residues: 22-128; Coverage: 84%)
Gene names: SAMN02910291_00073, cytc3
Sequence domains: Class III cytochrome C family
Structure domains: Cytochrome C3

Ligands and Environments

2 bound ligands:
Ligand HEC 4 x HEC
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P6122
Unit cell:
a: 61.49Å b: 61.49Å c: 105.66Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 0.24

Quick links

Citations

5 review citations

Understanding the mechanism of proton movement linked to oxygen reduction in cytochrome c oxidase: lessons from other proteins.
Mills et al. (2003)
4 more