3rwl

Structure of P450pyr hydroxylase

spinqualitylabelsall models 3rwl, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rwl is a 1 chain structure with sequence from Sphingopyxis macrogoltabida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5F4D9_SPHMC Publication Abstract from PubMed Directed evolution of a monooxygenase to achieve very high enantioselectivity for hydroxylation at non-activated carbon atoms is demonstrated for the first time, where a triple mutant of P450pyr hydroxylase is obtained via determination of enzyme structure, iterative saturation mutagenesis, and high-throughput screening with a MS-based ee assay to increase the product ee from 53% to 98% for the hydroxylation of N-benzyl pyrrolidine to (S)-N-benzyl 3-hydroxypyrrolidine. Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom.,Pham SQ, Pompidor G, Liu J, Li XD, Li Z Chem Commun (Camb). 2012 May 14;48(38):4618-20. Epub 2012 Mar 19. PMID:22430002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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