4HGI
Crystal structure of P450 BM3 5F5 heme domain variant complexed with styrene (dataset II)
Summary for 4HGI
Entry DOI | 10.2210/pdb4hgi/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 | 106329.78 |
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 Cited by PubMed: 23589805DOI: 10.1039/c3cc39076d PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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