1bvy

X-ray diffraction
2.03Å resolution

COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)

Released:
Source organism: Priestia 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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-147080 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 458 amino acids
Theoretical weight: 52.4 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 2-459; Coverage: 44%)
Gene names: BG04_163, cyp102, cyp102A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450
Bifunctional cytochrome P450/NADPH--P450 reductase Chain: F
Molecule details ›
Chain: F
Length: 191 amino acids
Theoretical weight: 20.8 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 460-650; Coverage: 18%)
Gene names: BG04_163, cyp102, cyp102A1
Sequence domains: Flavodoxin
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM

Cofactor: Ligand FMN 1 x FMN
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 58.84Å b: 94.68Å c: 209.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 not available 0.275
Expression system: Escherichia coli