› 1ccb

X-ray diffraction
2.1Å resolution

THE ASP-HIS-FE TRIAD OF CYTOCHROME C PEROXIDASE CONTROLS THE REDUCTION POTENTIAL, ELECTRONIC STRUCTURE, AND COUPLING OF THE TRYPTOPHAN FREE-RADICAL TO THE HEME

Released:
DOI: 10.2210/pdb1ccb/pdb
PDB entry 1ccb coloured by chain, front view.
PDB entry 1ccb coloured by chain, side view.
PDB entry 1ccb coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme.
Goodin DB, McRee DE
Biochemistry 32 3313-24 (1993)
PMID: 8384877

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: 297 amino acids
Theoretical weight: 33.9 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P00431 (Residues: 65-361; Coverage: 82%)
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

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Citations

15 review citations

Bacterial hemoglobins and flavohemoglobins: versatile proteins and their impact on microbiology and biotechnology.
Frey et al. (2003)
14 more