3wle
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3wle is ON HOLD Authors: Wang, S.S., Nie, Y., Xu, Y., Zhang, R.Z., Huang, C.H., Chan, H.C., Guo, R.T. , Xiao, R. Description: Complex structure of ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==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 with sequence from [https://en.wikipedia.org/wiki/Candida_parapsilosis Candida parapsilosis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3WLE FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.164Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wle OCA], [https://pdbe.org/3wle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wle RCSB], [https://www.ebi.ac.uk/pdbsum/3wle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wle ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A1X808_CANPA A1X808_CANPA] | ||
| + | <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> | ||
| + | <div class="pdbe-citations 3wle" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Candida parapsilosis]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chan HC]] | ||
| + | [[Category: Guo RT]] | ||
| + | [[Category: Huang CH]] | ||
| + | [[Category: Nie Y]] | ||
| + | [[Category: Wang SS]] | ||
| + | [[Category: Xiao R]] | ||
| + | [[Category: Xu Y]] | ||
| + | [[Category: Zhang RZ]] | ||
Current revision
Crystal structure of (R)-carbonyl reductase from Candida Parapsilosis in complex with NAD
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Categories: Candida parapsilosis | Large Structures | Chan HC | Guo RT | Huang CH | Nie Y | Wang SS | Xiao R | Xu Y | Zhang RZ
