PDBe 1krj

X-ray diffraction
2Å resolution

Engineering Calcium-binding site into Cytochrome c Peroxidase (CcP)

Released:

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: 33.66 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
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
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 107.034Å b: 75.458Å c: 51.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 not available
Expression system: Escherichia coli BL21(DE3)