› 6bww

X-ray diffraction
2.1Å resolution

Crystal structure of an acetate and Cymal-5 bound cytochrome P450 2B4 F429H mutant

Released:
DOI: 10.2210/pdb6bww/pdb
PDB entry 6bww coloured by chain, front view.
PDB entry 6bww coloured by chain, side view.
PDB entry 6bww coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structure of cytochrome P450 2B4 with an acetate ligand and an active site hydrogen bond network similar to oxyferrous P450cam.
Yang Y, Bu W, Im S, Meagher J, Stuckey J, Waskell L
J Inorg Biochem 185 17-25 (2018)
PMID: 29730233

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 Chain: A
Molecule details ›
Chain: A
Length: 472 amino acids
Theoretical weight: 53.62 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00178 (Residues: 30-491; Coverage: 94%)
Gene name: CYP2B4
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
3 bound ligands:
Ligand CM5 2 x CM5
Ligand ACT 8 x ACT
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P3121
Unit cell:
a: 93.185Å b: 93.185Å c: 151.092Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.185 0.206
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Low-Temperature Selective Catalytic Reduction of NO x with NH3 over Mn-Ce Composites Synthesized by Polymer-Assisted Deposition.
Xiao et al. (2021)

1 mention without citation

Structure of cytochrome P450 2B4 with an acetate ligand and an active site hydrogen bond network similar to oxyferrous P450cam.
Yang et al. (2018)