3wlf

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

Structural highlights

3wlf is a 4 chain structure with sequence from Candida parapsilosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:FEH, ZN
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A1X808_CANPA

Publication Abstract from PubMed

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.

Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase.,Wang S, Nie Y, Xu Y, Zhang R, Ko TP, Huang CH, Chan HC, Guo RT, Xiao R Chem Commun (Camb). 2014 Jun 24;50(58):7770-2. doi: 10.1039/c4cc01752h. PMID:24834985[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. ↑ Wang S, Nie Y, Xu Y, Zhang R, Ko TP, Huang CH, Chan HC, Guo RT, Xiao R. Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase. Chem Commun (Camb). 2014 Jun 24;50(58):7770-2. doi: 10.1039/c4cc01752h. PMID:24834985 doi:http://dx.doi.org/10.1039/c4cc01752h

Contents


PDB ID 3wlf

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OCA

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