› 3wsp

X-ray diffraction
1.8Å resolution

Crystal Structure of P450BM3 with N-perfluorononanoyl-L-tryptophan

Released:
DOI: 10.2210/pdb3wsp/pdb
PDB entry 3wsp coloured by chain, front view.
PDB entry 3wsp coloured by chain, side view.
PDB entry 3wsp coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Activation of Wild-type Cytochrome P450BM3 by the Next Generation of Decoy Molecules: Enhanced Hydroxylation of Gaseous Alkanes and Crystallographic Evidence.
Cong Z, Shoji O, Kasai C, Kawakami N, Sugimoto H, Shiro Y, Watanabe Y
ACS Catalysis 5 150-156 (2015)

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 456 amino acids
Theoretical weight: 52.3 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 1-456; Coverage: 44%)
Gene names: BG04_163, cyp102, cyp102A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:
Ligand W09 2 x W09
Ligand DMS 2 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 58.875Å b: 145.392Å c: 63.029Å
α: 90° β: 97.06° γ: 90°
R-values:
R R work R free
0.176 0.174 0.212
Expression system: Escherichia coli

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