› 1smi

X-ray diffraction
2Å resolution

A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme

Released:
DOI: 10.2210/pdb1smi/pdb
PDB entry 1smi coloured by chain, front view.
PDB entry 1smi coloured by chain, side view.
PDB entry 1smi coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
A single mutation in cytochrome P450 BM3 induces the conformational rearrangement seen upon substrate binding in the wild-type enzyme.
Joyce MG, Girvan HM, Munro AW, Leys D
J Biol Chem 279 23287-93 (2004)
PMID: 15020590

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: 471 amino acids
Theoretical weight: 53.85 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 2-472; 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
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 61.206Å b: 118.929Å c: 146.338Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.224 0.288
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

1 mention without citation

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