X-ray diffraction
1.82Å resolution

Cyrstal Structure of Cytochrome c Peroxidase Mutant: CcPK2M3

Source organism: Saccharomyces cerevisiae
Primary publication:
Electrostatic control of the tryptophan radical in cytochrome c peroxidase.
Biochemistry 43 8826-34 (2004)
PMID: 15236591

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
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.6 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P00431 (Residues: 68-361; Coverage: null%)
Gene names: CCP, CCP1, CPO, YKR066C
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 106.788Å b: 75.692Å c: 51.281Å
α: 90° β: 90° γ: 90°
R R work R free
0.2 0.192 0.216
Expression system: Escherichia coli BL21(DE3)