3WNQ

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

3WNQ の概要

• エントリーDOI: 10.2210/pdb3wnq/pdb
• 分子名称: (R)-specific carbonyl reductase, 2-hydroxy-1-phenylethanone, ZINC ION, ... (4 entities in total)
• 機能のキーワード: alcohol dehydrogenase, carbonyl reductase, oxidoreductase
• 由来する生物種: Candida parapsilosis (Yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 146185.78

構造登録者

Wang, S.S.,Nie, Y.,Xu, Y.,Zhang, R.Z.,Huang, C.H.,Chan, H.C.,Guo, R.T.,Ko, T.P.,Xiao, R. (登録日: 2013-12-15, 公開日: 2014-07-16, 最終更新日: 2023-11-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.95 Å)