PDBe 1dcc

X-ray diffraction
2.2Å resolution

2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex.
Nat. Struct. Biol. 1 524-31 (1994)
PMID: 7664080

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: 296 amino acids
Theoretical weight: 33.73 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P00431 (Residues: 68-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 104.722Å b: 74.446Å c: 45.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 not available not available
Expression system: Not provided