3WNQ

Crystal structure of (R)-carbonyl reductase H49A mutant from Candida Parapsilosis in complex with 2-hydroxyacetophenone

Summary for 3WNQ

Entry DOI	10.2210/pdb3wnq/pdb
Descriptor	(R)-specific carbonyl reductase, 2-hydroxy-1-phenylethanone, ZINC ION, ... (4 entities in total)
Functional Keywords	alcohol dehydrogenase, carbonyl reductase, oxidoreductase
Biological source	Candida parapsilosis (Yeast)
Total number of polymer chains	4
Total formula weight	146185.78
Authors	Wang, S.S.,Nie, Y.,Xu, Y.,Zhang, R.Z.,Huang, C.H.,Chan, H.C.,Guo, R.T.,Ko, T.P.,Xiao, R. (deposition date: 2013-12-15, release date: 2014-07-16, Last modification date: 2023-11-08)
Primary citation	Wang, S.S.,Nie, Y.,Xu, Y.,Zhang, R.Z.,Ko, T.P.,Huang, C.H.,Chan, H.C.,Guo, R.T.,Xiao, R. Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase Chem.Commun.(Camb.), 50:7770-7772, 2014 Cited by PubMed Abstract: Structure-guided design of substrate-binding pocket inversed the stereoselectivity of an NADH-dependent medium-chain alcohol dehydrogenase (MDR) from Prelog to anti-Prelog. The pocket-forming amino acids, especially the unconserved residues as hotspots, play critical roles in directing MDRs' stereoselectivity. PubMed: 24834985 DOI: 10.1039/c4cc01752h PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.95 Å)

Structure validation