› 1ebe

X-ray diffraction
2.2Å resolution

Laue diffraction study on the structure of cytochrome c peroxidase compound I

Released:
DOI: 10.2210/pdb1ebe/pdb
PDB entry 1ebe coloured by chain, front view.
PDB entry 1ebe coloured by chain, side view.
PDB entry 1ebe coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Laue diffraction study on the structure of cytochrome c peroxidase compound I.
Fülöp V, Phizackerley RP, Soltis SM, Clifton IJ, Wakatsuki S, Erman J, Hajdu J, Edwards SL
Structure 2 201-8 (1994)
PMID: 8069633

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: 294 amino acids
Theoretical weight: 33.57 KDa
Source organism: Saccharomyces cerevisiae
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 O 1 x O
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS
Spacegroup: P212121
Unit cell:
a: 107.4Å b: 76.8Å c: 51.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.144 not available

Quick links

Citations

10 review citations

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

1 mention without citation

Local Electric Fields as a Natural Switch of Heme-Iron Protein Reactivity.
Bím et al. (2021)