› 1cpq

X-ray diffraction
1.72Å resolution

CYTOCHROME C' FROM RHODOPSEUDOMONAS CAPSULATA

Released:
DOI: 10.2210/pdb1cpq/pdb
PDB entry 1cpq coloured by chain, front view.
PDB entry 1cpq coloured by chain, side view.
PDB entry 1cpq coloured by chain, top view.
Source organism: Rhodobacter capsulatus
Primary publication:
High-resolution crystal structures of two polymorphs of cytochrome c' from the purple phototrophic bacterium rhodobacter capsulatus.
Tahirov TH, Misaki S, Meyer TE, Cusanovich MA, Higuchi Y, Yasuoka N
J Mol Biol 259 467-79 (1996)
PMID: 8676382

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132289 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c' Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 13.15 KDa
Source organism: Rhodobacter capsulatus
UniProt:
  • Canonical: P00147 (Residues: 1-129; Coverage: 100%)
Sequence domains: Cytochrome C'
Structure domains: Cytochrome c/b562

Ligands and Environments

1 bound ligand:
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P21212
Unit cell:
a: 47.82Å b: 72.59Å c: 34.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.15 not available

Quick links

Citations

2 review citations

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
1 more

5 mentions without citation

The chemistry and biochemistry of heme c: functional bases for covalent attachment.
Bowman et al. (2008)
4 more