Crystal structure of P450 BM3 5F5 heme domain variantCrystal structure of P450 BM3 5F5 heme domain variant

Structural highlights

4hgj is a 2 chain structure with sequence from Bacillus megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:cyp102, cyp102A1 (Bacillus megaterium)
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

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.

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 Also

References

  1. 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). 2013 May 21;49(41):4694-6. doi: 10.1039/c3cc39076d. Epub 2013, Apr 15. PMID:23589805 doi:http://dx.doi.org/10.1039/c3cc39076d

4hgj, resolution 1.90Å

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