› 1cpd

X-ray diffraction
2.2Å resolution

A CATION BINDING MOTIF STABILIZES THE COMPOUND I RADICAL OF CYTOCHROME C PEROXIDASE

Released:
DOI: 10.2210/pdb1cpd/pdb
PDB entry 1cpd coloured by chain, front view.
PDB entry 1cpd coloured by chain, side view.
PDB entry 1cpd coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A cation binding motif stabilizes the compound I radical of cytochrome c peroxidase.
Miller MA, Han GW, Kraut J
Proc Natl Acad Sci U S A 91 11118-22 (1994)
PMID: 7972020

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132475 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 296 amino acids
Theoretical weight: 33.64 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


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand NH4 1 x NH4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 105Å b: 74.2Å c: 45.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
1 more

1 mention without citation

Orientation tuning in the visual cortex of 3-month-old human infants.
Baker et al. (2011)