› 1zo9

X-ray diffraction
1.7Å resolution

Crystal Structure Of The Wild Type Heme Domain Of P450BM-3 with N-palmitoylmethionine

Released:
DOI: 10.2210/pdb1zo9/pdb
PDB entry 1zo9 coloured by chain, front view.
PDB entry 1zo9 coloured by chain, side view.
PDB entry 1zo9 coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Interactions of substrates at the surface of P450s can greatly enhance substrate potency.
Hegde A, Haines DC, Bondlela M, Chen B, Schaffer N, Tomchick DR, Machius M, Nguyen H, Chowdhary PK, Stewart L, Lopez C, Peterson JA
Biochemistry 46 14010-7 (2007)
PMID: 18004886

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 domain:

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: 53.9 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
3 bound ligands:
Ligand EPM 2 x EPM
Ligand GOL 14 x GOL
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 59.039Å b: 147.807Å c: 63.604Å
α: 90° β: 98.6° γ: 90°
R-values:
R R work R free
0.199 0.164 0.199
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

3 mentions without citation

Potentially increasing the metabolic stability of drug candidates via computational site of metabolism prediction by CYP2C9: The utility of incorporating protein flexibility via an ensemble of structures.
Danielson et al. (2011)
2 more