1yqo

X-ray diffraction
1.9Å resolution

T268A mutant heme domain of flavocytochrome P450 BM3

Released:
Source organism: Priestia megaterium
Primary publication:
The role of Thr268 and Phe393 in cytochrome P450 BM3.
J Inorg Biochem 100 1075-90 (2006)
PMID: 16403573

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 455 amino acids
Theoretical weight: 52.14 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: SRS BEAMLINE PX14.1
Spacegroup: P21
Unit cell:
a: 58.727Å b: 152.962Å c: 61.732Å
α: 90° β: 94.37° γ: 90°
R-values:
R R work R free
0.168 0.166 0.206
Expression system: Escherichia coli