› 1cce

X-ray diffraction
2.3Å resolution

CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND

Released:
DOI: 10.2210/pdb1cce/pdb
PDB entry 1cce coloured by chain, front view.
PDB entry 1cce coloured by chain, side view.
PDB entry 1cce coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Construction of a bisaquo heme enzyme and binding by exogenous ligands.
McRee DE, Jensen GM, Fitzgerald MM, Siegel HA, Goodin DB
Proc Natl Acad Sci U S A 91 12847-51 (1994)
PMID: 7809133

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: 291 amino acids
Theoretical weight: 33.14 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P00431 (Residues: 71-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 105.2Å b: 74.3Å c: 45.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

Quick links

Citations

5 review citations

Diversity and conservation of interactions for binding heme in b-type heme proteins.
Schneider et al. (2007)
4 more

1 mention without citation

Impact of Proximal and Distal Pocket Site-Directed Mutations on the Ferric/Ferrous Heme Redox Potential of Yeast Cytochrome-c-Peroxidase.
Jensen et al. (2011)