4hgf | pdb_00004hgf
From Proteopedia
Crystal structure of P450 BM3 5F5K heme domain variant complexed with styrene
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Structural highlights
Publication Abstract from PubMedSolved crystal structures of P450 BM3 variants in complex with styrene provide on the molecular level a first explanation of how a positively charged surface residue inverts the enantiopreference of styrene epoxidation. The obtained insights into productive and non-productive styrene binding modes deepened our understanding of enantioselective epoxidation with P450 BM3. P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation.,Shehzad A, Panneerselvam S, Linow M, Bocola M, Roccatano D, Mueller-Dieckmann J, Wilmanns M, Schwaneberg U Chem Commun (Camb). 2013 May 21;49(41):4694-6. doi: 10.1039/c3cc39076d. Epub 2013, Apr 15. PMID:23589805[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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This page was last modified 12:41, 21 December 2014.