3wle
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Crystal structure of (R)-carbonyl reductase from Candida Parapsilosis in complex with NAD== |
+ | <StructureSection load='3wle' size='340' side='right' caption='[[3wle]], [[Resolution|resolution]] 2.16Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3wle]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WLE FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wlf|3wlf]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wle RCSB], [http://www.ebi.ac.uk/pdbsum/3wle PDBsum]</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Alcohol dehydrogenase]] | ||
+ | [[Category: Chan, H C.]] | ||
+ | [[Category: Guo, R T.]] | ||
+ | [[Category: Huang, C H.]] | ||
+ | [[Category: Nie, Y.]] | ||
+ | [[Category: Wang, S S.]] | ||
+ | [[Category: Xiao, R.]] | ||
+ | [[Category: Xu, Y.]] | ||
+ | [[Category: Zhang, R Z.]] | ||
+ | [[Category: Alcohol dehydrogenase]] | ||
+ | [[Category: Carbonyl reductase]] | ||
+ | [[Category: Oxidoreductase]] |
Revision as of 10:19, 16 July 2014
Crystal structure of (R)-carbonyl reductase from Candida Parapsilosis in complex with NAD
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