› 1p0x

X-ray diffraction
2Å resolution

F393Y mutant heme domain of flavocytochrome P450 BM3

Released:
DOI: 10.2210/pdb1p0x/pdb
PDB entry 1p0x coloured by chain, front view.
PDB entry 1p0x coloured by chain, side view.
PDB entry 1p0x coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Oxygen activation and electron transfer in flavocytochrome P450 BM3.
Ost TW, Clark J, Mowat CG, Miles CS, Walkinshaw MD, Reid GA, Chapman SK, Daff S
J Am Chem Soc 125 15010-20 (2003)
PMID: 14653735

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional cytochrome P450/NADPH--P450 reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 52.19 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: P14779 (Residues: 2-456; Coverage: 43%)
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: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 59.608Å b: 152.983Å c: 61.774Å
α: 90° β: 94.54° γ: 90°
R-values:
R R work R free
0.172 0.172 0.237
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Update on mechanism and catalytic regulation in the NO synthases.
Stuehr et al. (2004)
11 more