› 1vng

X-ray diffraction
2.2Å resolution

CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS: MUTANT H404A

Released:
DOI: 10.2210/pdb1vng/pdb
PDB entry 1vng coloured by chain, front view.
PDB entry 1vng coloured by chain, side view.
PDB entry 1vng coloured by chain, top view.
Source organism: Curvularia inaequalis
Primary publication:
X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis.
Macedo-Ribeiro S, Hemrika W, Renirie R, Wever R, Messerschmidt A
J Biol Inorg Chem 4 209-19 (1999)
PMID: 10499093

Function and Biology Details

Reaction catalysed: 
RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vanadium chloroperoxidase Chain: A
Molecule details ›
Chain: A
Length: 609 amino acids
Theoretical weight: 67.56 KDa
Source organism: Curvularia inaequalis
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P49053 (Residues: 1-609; Coverage: 100%)
Gene name: CPO
Sequence domains: Vanadium chloroperoxidase N-terminal domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand VO4 1 x VO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R3
Unit cell:
a: 129.6Å b: 129.6Å c: 104.45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.21
Expression system: Saccharomyces cerevisiae

Quick links

Citations

6 review citations

Integral membrane lipid phosphatases/phosphotransferases: common structure and diverse functions.
Sigal et al. (2005)
5 more

3 mentions without citation

Halogenases: a palette of emerging opportunities for synthetic biology-synthetic chemistry and C-H functionalisation.
Crowe et al. (2021)
2 more