› 1izo

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
Fatty acid + H(2)O(2) = 3- or 2-hydroxy fatty acid + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty-acid peroxygenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 417 amino acids
Theoretical weight: 48.18 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O31440 (Residues: 1-417; Coverage: 100%)
Gene names: BSU02100, CYP152A1, cypC
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 3 x HEM
1 bound ligand:
Ligand PAM 3 x PAM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P3221
Unit cell:
a: 155.789Å b: 155.789Å c: 111.904Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.246 0.246 0.28
Expression system: Escherichia coli

Quick links

Citations

27 review citations

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

14 mentions without citation

Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.
Huang et al. (2018)
13 more