4HGH

Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset I)

Summary for 4HGH

• Entry DOI: 10.2210/pdb4hgh/pdb
• Related: 1BU7 1JPZ
• Descriptor: Bifunctional P-450/NADPH-P450 reductase, PROTOPORPHYRIN IX CONTAINING FE, ethenylbenzene, ... (7 entities in total)
• Functional Keywords: oxidoreductase, p450 bm3, hemoprotein, styrene epoxidation, inverted enantioselectivity, heme binding
• Biological source: Bacillus megaterium
• Cellular location: Cytoplasm (By similarity): P14779
• Total number of polymer chains: 2
• Total formula weight: 106248.73

Authors

Shehzad, A.,Panneerselvam, S.,Bocola, M.,Mueller-Dieckmann, J.,Wilmanns, M.,Schwaneberg, U. (deposition date: 2012-10-08, release date: 2013-05-01, Last modification date: 2023-09-20)

Primary citation

Shehzad, A.,Panneerselvam, S.,Linow, M.,Bocola, M.,Roccatano, D.,Mueller-Dieckmann, J.,Wilmanns, M.,Schwaneberg, U.
P450 BM3 crystal structures reveal the role of the charged surface residue Lys/Arg184 in inversion of enantioselective styrene epoxidation.
Chem.Commun.(Camb.), 49:4694-4696, 2013

PubMed Abstract: Solved 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.

PubMed: 23589805
DOI: 10.1039/c3cc39076d

Experimental method

X-RAY DIFFRACTION (1.4 Å)