View source for 3wnq


==Crystal structure of (R)-carbonyl reductase H49A mutant from Candida Parapsilosis in complex with 2-hydroxyacetophenone==
<StructureSection load='3wnq' size='340' side='right'caption='[[3wnq]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wnq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_22019 Atcc 22019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WNQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HXT:2-HYDROXY-1-PHENYLETHANONE'>HXT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rCR, CPRADH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5480 ATCC 22019])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wnq OCA], [https://pdbe.org/3wnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wnq RCSB], [https://www.ebi.ac.uk/pdbsum/3wnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wnq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== 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<ref>PMID:24834985</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wnq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alcohol dehydrogenase]]
[[Category: Atcc 22019]]
[[Category: Large Structures]]
[[Category: Chan, H C]]
[[Category: Guo, R T]]
[[Category: Huang, C H]]
[[Category: Ko, T P]]
[[Category: Nie, Y]]
[[Category: Wang, S S]]
[[Category: Xiao, R]]
[[Category: Xu, Y]]
[[Category: Zhang, R Z]]
[[Category: Carbonyl reductase]]
[[Category: Oxidoreductase]]