4dgq

X-ray diffraction
1.85Å resolution

Crystal structure of Non-heme chloroperoxidase from Burkholderia cenocepacia

Released:
Entry authors: Gardberg AS, Edwards TE, Abendroth JA, Staker B, Stewart L, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-110015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 280 amino acids
Theoretical weight: 30.58 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B4EA96 (Residues: 1-276; Coverage: 100%)
Gene names: BCAL0771, cpo
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 60.77Å b: 111.85Å c: 80.21Å
α: 90° β: 111.65° γ: 90°
R-values:
R R work R free
0.136 0.135 0.163
Expression system: Escherichia coli BL21(DE3)