› 2vhd

X-ray diffraction
2.3Å resolution

Crystal Structure Of The Di-Haem Cytochrome C Peroxidase From Pseudomonas aeruginosa - Mixed Valence Form

Released:
DOI: 10.2210/pdb2vhd/pdb
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Source organism: Pseudomonas aeruginosa
Primary publication:
Redox-linked structural changes associated with the formation of a catalytically competent form of the diheme cytochrome c peroxidase from Pseudomonas aeruginosa.
Echalier A, Brittain T, Wright J, Boycheva S, Mortuza GB, Fülöp V, Watmough NJ
Biochemistry 47 1947-56 (2008)
PMID: 18217775

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c551 peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 35.08 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P14532 (Residues: 24-346; Coverage: 100%)
Gene names: PA4587, ccpA
Sequence domains:
Structure domains: Cytochrome c-like domain

Ligands and Environments


Cofactor: Ligand HEC 4 x HEC
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 173.2Å b: 44.8Å c: 106.2Å
α: 90° β: 106.7° γ: 90°
R-values:
R R work R free
0.187 0.184 0.246
Expression system: Escherichia coli

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Citations

5 review citations

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

5 mentions without citation

Multi-heme proteins: nature's electronic multi-purpose tool.
Bewley et al. (2013)
4 more

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