PDBe 1bu7

X-ray diffraction
1.65Å resolution

CRYOGENIC STRUCTURE OF CYTOCHROME P450BM-3 HEME DOMAIN

Released:
Source organism: Bacillus megaterium
Primary publication:
Structure of a cytochrome P450-redox partner electron-transfer complex.
Proc. Natl. Acad. Sci. U.S.A. 96 1863-8 (1999)
PMID: 10051560

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 52.17 KDa
Source organism: Bacillus megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 2-456; Coverage: 43%)
Gene names: BG04_163, cyp102, cyp102A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome p450

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 59.38Å b: 151.9Å c: 62.77Å
α: 90° β: 96.02° γ: 90°
R-values:
R R work R free
0.197 not available 0.251
Expression system: Escherichia coli