› 3m4v

X-ray diffraction
1.9Å resolution

Crystal structure of the A330P mutant of cytochrome P450 BM3

Released:
DOI: 10.2210/pdb3m4v/pdb
PDB entry 3m4v coloured by chain, front view.
PDB entry 3m4v coloured by chain, side view.
PDB entry 3m4v coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Structural basis for the properties of two single-site proline mutants of CYP102A1 (P450BM3).
Whitehouse CJ, Yang W, Yorke JA, Rowlatt BC, Strong AJ, Blanford CF, Bell SG, Bartlam M, Wong LL, Rao Z
Chembiochem 11 2549-56 (2010)
PMID: 21110374

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: 482 amino acids
Theoretical weight: 55.05 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 1-482; Coverage: 46%)
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
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 58.542Å b: 148.281Å c: 64.368Å
α: 90° β: 99.93° γ: 90°
R-values:
R R work R free
0.189 0.187 0.232
Expression system: Escherichia coli

Quick links

Citations

2 review citations

P450(BM3) (CYP102A1): connecting the dots.
Whitehouse et al. (2012)
1 more

1 mention without citation

Molecular Determinants of Substrate Affinity and Enzyme Activity of a Cytochrome P450BM3 Variant.
Geronimo et al. (2018)