We've built a new version of this page with an interactive 3D viewer. Try it out in beta and help us improve:

› 3ben

X-ray diffraction
1.65Å resolution

Structure of N-(12-imidazolyl-dodecanoyl)-L-leucine inhibitor bound to the heme domain of Cytochrome P450-BM3

Released:
DOI: 10.2210/pdb3ben/pdb
Model geometry
Fit model/data
PDB entry 3ben coloured by chain, front view.
PDB entry 3ben coloured by chain, side view.
PDB entry 3ben coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of substrate access channel.
Haines DC, Chen B, Tomchick DR, Bondlela M, Hegde A, Machius M, Peterson JA
Biochemistry 47 3662-70 (2008)
PMID: 18298086

Function and Biology Details

Reactions catalysed: 
an organic molecule + reduced [NADPH--hemoprotein reductase] + O2 =an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+).
2 oxidized [cytochrome P450] + NADPH = 2 reduced [cytochrome P450] +NADP(+) + H(+).
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: 470 amino acids
Theoretical weight: 53.67 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 1-470; 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 LEH 2 x LEH
Ligand MG 1 x MG
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 58.82Å b: 148.209Å c: 63.792Å
α: 90° β: 98.32° γ: 90°
R-values:
R R work R free
0.162 0.161 0.191
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

2 mentions without citation

Conformational plasticity and structure/function relationships in cytochromes P450.
Pochapsky et al. (2010)
1 more