2xj5

X-ray diffraction
1.69Å resolution

The structure of cytochrome c peroxidase Compound II

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Nature of the ferryl heme in compounds I and II.
J. Biol. Chem. 286 1260-8 (2011)
PMID: 21062738

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.63 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00431 (Residues: 71-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 51.05Å b: 75.139Å c: 106.919Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.197
Expression system: Escherichia coli BL21(DE3)