X-ray diffraction
2Å resolution

F393W mutant heme domain of flavocytochrome P450 BM3

Source organism: Bacillus megaterium

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 52.21 KDa
Source organism: Bacillus megaterium
Expression system: Escherichia coli
  • Canonical: P14779 (Residues: 2-456; Coverage: 43%)
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: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 58.911Å b: 153.538Å c: 61.43Å
α: 90° β: 94.42° γ: 90°
R R work R free
0.159 0.159 0.221
Expression system: Escherichia coli