PDBe 1cck

X-ray diffraction
2.1Å resolution

ALTERING SUBSTRATE SPECIFICITY OF CYTOCHROME C PEROXIDASE TOWARDS A SMALL MOLECULAR SUBSTRATE PEROXIDASE BY SUBSTITUTING TYROSINE FOR PHE 202

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of recombinant pea cytosolic ascorbate peroxidase.
Biochemistry 34 4331-41 (1995)
PMID: 7703247

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: 291 amino acids
Theoretical weight: 33.24 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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 103.5Å b: 73.4Å c: 44.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 not available
Expression system: Escherichia coli BL21(DE3)