X-ray diffraction
3.4Å resolution

Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3


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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 455 amino acids
Theoretical weight: 52.17 KDa
Source organism: Bacillus megaterium
Expression system: Escherichia coli BL21(DE3)
  • 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 MNH 4 x MNH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: C2221
Unit cell:
a: 104.76Å b: 155.32Å c: 208.98Å
α: 90° β: 90° γ: 90°
R R work R free
0.312 0.31 0.346
Expression system: Escherichia coli BL21(DE3)