3WLF

Crystal structure of (R)-carbonyl reductase from Candida Parapsilosis in complex with (R)-1-phenyl-1,2-ethanediol

Summary for 3WLF

• Entry DOI: 10.2210/pdb3wlf/pdb
• Related: 3WLE
• Descriptor: (R)-specific carbonyl reductase, (1R)-1-phenylethane-1,2-diol, 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: 146462.13

Authors

Wang, S.S.,Nie, Y.,Xu, Y.,Zhang, R.Z.,Huang, C.H.,Chan, H.C.,Guo, R.T.,Xiao, R. (deposition date: 2013-11-09, 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

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)