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Structure paper

TitleP450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation.
Journal, issue, pagesChem. Commun. (Camb. ), Vol. 49, Page 4694-4696, Year 2013
Publish dateOct 8, 2012 (structure data deposition date)
AuthorsShehzad, A. / Panneerselvam, S. / Linow, M. / Bocola, M. / Roccatano, D. / Mueller-Dieckmann, J. / Wilmanns, M. / Schwaneberg, U.
External linksChem. Commun. (Camb. ) / PubMed:23589805
MethodsX-ray diffraction
Resolution1.4 - 1.9 Å
Structure data

PDB-4hgf:
Crystal structure of P450 BM3 5F5K heme domain variant complexed with styrene
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4hgg:
Crystal structure of P450 BM3 5F5R heme domain variant complexed with styrene
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-4hgh:
Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset I)
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-4hgi:
Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset II)
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-4hgj:
Crystal structure of P450 BM3 5F5 heme domain variant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-SYN:
ethenylbenzene

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-GOL:
GLYCEROL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • bacillus megaterium (bacteria)
KeywordsOXIDOREDUCTASE / P450 BM3 / hemoprotein / styrene epoxidation / inverted enantioselectivity / Heme binding

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