› 1bva

X-ray diffraction
1.89Å resolution

MANGANESE BINDING MUTANT IN CYTOCHROME C PEROXIDASE

Released:
DOI: 10.2210/pdb1bva/pdb
PDB entry 1bva coloured by chain, front view.
PDB entry 1bva coloured by chain, side view.
PDB entry 1bva coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Rational design of a functional metalloenzyme: introduction of a site for manganese binding and oxidation into a heme peroxidase.
Wilcox SK, Putnam CD, Sastry M, Blankenship J, Chazin WJ, McRee DE, Goodin DB
Biochemistry 37 16853-62 (1998)
PMID: 9836578

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: 33.64 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


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P212121
Unit cell:
a: 105.8Å b: 73.6Å c: 50.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 not available not available
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Protein design: toward functional metalloenzymes.
Yu et al. (2014)
4 more