› 1zo4

X-ray diffraction
1.46Å resolution

Crystal Structure Of A328S Mutant Of The Heme Domain Of P450BM-3

Released:
DOI: 10.2210/pdb1zo4/pdb
Model geometry
Fit model/data
PDB entry 1zo4 coloured by chain, front view.
PDB entry 1zo4 coloured by chain, side view.
PDB entry 1zo4 coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation.
Haines DC, Hegde A, Chen B, Zhao W, Bondlela M, Humphreys JM, Mullin DA, Tomchick DR, Machius M, Peterson JA
Biochemistry 50 8333-41 (2011)
PMID: 21875028

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: 473 amino acids
Theoretical weight: 53.91 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 2-471; Coverage: 45%)
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 MES 2 x MES
Ligand GOL 20 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 58.827Å b: 153.209Å c: 61.583Å
α: 90° β: 94.33° γ: 90°
R-values:
R R work R free
0.216 0.189 0.216
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Optimization of the bacterial cytochrome P450 BM3 system for the production of human drug metabolites.
Di Nardo et al. (2012)
7 other articles

2 mentions without citation

Structural basis for androgen specificity and oestrogen synthesis in human aromatase.
Ghosh et al. (2009)
1 more