› 3tk3

X-ray diffraction
2.8Å resolution

Cytochrome P450 2B4 mutant L437A in complex with 4-(4-chlorophenyl)imidazole

Released:
DOI: 10.2210/pdb3tk3/pdb
PDB entry 3tk3 coloured by chain, front view.
PDB entry 3tk3 coloured by chain, side view.
PDB entry 3tk3 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein-ligand interactions based on crystal structures of the ligand-bound enzyme.
Wilderman PR, Gay SC, Jang HH, Zhang Q, Stout CD, Halpert JR
FEBS J 279 1607-20 (2012)
PMID: 22051155

Function and Biology Details

Reaction catalysed: 
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132309 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 2B4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 476 amino acids
Theoretical weight: 54.13 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00178 (Residues: 20-491; Coverage: 96%)
Gene name: CYP2B4
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
Ligand CPZ 4 x CPZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P3
Unit cell:
a: 232.91Å b: 232.91Å c: 56.96Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.193 0.241
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Substrate tunnels in enzymes: structure-function relationships and computational methodology.
Kingsley et al. (2015)
5 more

4 mentions without citation

Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein-ligand interactions based on crystal structures of the ligand-bound enzyme.
Wilderman et al. (2012)
3 more