› 1rz5

X-ray diffraction
2.4Å resolution

Di-haem Cytochrome c Peroxidase, Form OUT

Released:
DOI: 10.2210/pdb1rz5/pdb
PDB entry 1rz5 coloured by chain, front view.
PDB entry 1rz5 coloured by chain, side view.
PDB entry 1rz5 coloured by chain, top view.
Source organism: Marinobacter nauticus
Primary publication:
Structural basis for the mechanism of Ca(2+) activation of the di-heme cytochrome c peroxidase from Pseudomonas nautica 617.
Dias JM, Alves T, Bonifácio C, Pereira AS, Trincão J, Bourgeois D, Moura I, Romão MJ
Structure 12 961-73 (2004)
PMID: 15274917

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-160740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 35.38 KDa
Source organism: Marinobacter nauticus
UniProt:
  • Canonical: P83787 (Residues: 1-326; Coverage: 100%)
Sequence domains:
Structure domains: Cytochrome c-like domain

Ligands and Environments


Cofactor: Ligand HEC 2 x HEC
1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P6422
Unit cell:
a: 150.553Å b: 150.553Å c: 155.349Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.186 0.209

Quick links

Citations

6 review citations

Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
Pettigrew et al. (2006)
5 more

2 mentions without citation

Investigating the local flexibility of functional residues in hemoproteins.
Sacquin-Mora et al. (2006)
1 more