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TitleGlutamate-haem ester bond formation is disfavoured in flavocytochrome P450 BM3: characterization of glutamate substitution mutants at the haem site of P450 BM3.
Journal, issue, pagesBiochem. J., Vol. 427, Page 455-466, Year 2010
Publish dateDec 2, 2009 (structure data deposition date)
AuthorsGirvan, H.M. / Levy, C.W. / Williams, P. / Fisher, K. / Cheesman, M.R. / Rigby, S.E. / Leys, D. / Munro, A.W.
External linksBiochem. J. / PubMed:20180779
MethodsX-ray diffraction
Resolution1.686 - 1.95 Å
Structure data

PDB-3kx3:
Crystal structure of Bacillus megaterium BM3 heme domain mutant L86E
Method: X-RAY DIFFRACTION / Resolution: 1.803 Å

PDB-3kx4:
Crystal structure of Bacillus megaterium BM3 heme domain mutant I401E
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-3kx5:
Crystal structure of Bacillus megaterium BM3 heme domain mutant F261E
Method: X-RAY DIFFRACTION / Resolution: 1.686 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-140:
N-PALMITOYLGLYCINE

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • bacillus megaterium (bacteria)
KeywordsOXIDOREDUCTASE / cytochrome P450 / L86E mutant / Heme domain / Cytoplasm / Electron transport / FAD / Flavoprotein / FMN / Heme / Iron / Metal-binding / Monooxygenase / Multifunctional enzyme / NADP / Transport / I401E mutant / F261E mutant

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