3hf2

X-ray diffraction
2.2Å resolution

Crystal structure of the I401P mutant of cytochrome P450 BM3

Released:

Function and Biology Details

Reactions catalysed:
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
NADPH + n oxidized hemoprotein = NADP(+) + n reduced hemoprotein
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-147083 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 482 amino acids
Theoretical weight: 55.01 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 1-482; Coverage: 46%)
Gene names: BG04_163, cyp102, cyp102A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 58.67Å b: 145.843Å c: 63.229Å
α: 90° β: 97.33° γ: 90°
R-values:
R R work R free
0.189 0.186 0.245
Expression system: Escherichia coli