2bmh

X-ray diffraction
2Å resolution

MODELING PROTEIN-SUBSTRATE INTERACTIONS IN THE HEME DOMAIN OF CYTOCHROME P450BM-3

Released:
Source organism: Bacillus megaterium
Primary publication:
Modeling protein-substrate interactions in the heme domain of cytochrome P450(BM-3).
Acta Crystallogr. D Biol. Crystallogr. 51 21-32 (1995)
PMID: 15299332

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
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: Not provided
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


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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 59.53Å b: 154.03Å c: 62.43Å
α: 90° β: 94.97° γ: 90°
R-values:
R R work R free
0.184 0.184 not available
Expression system: Not provided