3RWL

Structure of P450pyr hydroxylase

Summary for 3RWL

Entry DOI	10.2210/pdb3rwl/pdb
Descriptor	Cytochrome P450 alkane hydroxylase 1 CYP153A7, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywords	p450 monooxygenase, oxidoreductase
Biological source	Sphingopyxis macrogoltabida
Total number of polymer chains	1
Total formula weight	48875.05
Authors	Pompidor, G. (deposition date: 2011-05-09, release date: 2012-04-18, Last modification date: 2024-02-28)
Primary citation	Pham, S.Q.,Pompidor, G.,Liu, J.,Li, X.D.,Li, Z. Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom. Chem.Commun.(Camb.), 48:4618-4620, 2012 Cited by PubMed Abstract: 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. PubMed: 22430002 DOI: 10.1039/c2cc30779k PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation