3wlf: Difference between revisions

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New page: '''Unreleased structure''' The entry 3wlf 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'''


The entry 3wlf is ON HOLD
==Crystal structure of (R)-carbonyl reductase from Candida Parapsilosis in complex with (R)-1-phenyl-1,2-ethanediol==
<StructureSection load='3wlf' size='340' side='right'caption='[[3wlf]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wlf]] 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=3WLF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WLF 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEH:(1R)-1-PHENYLETHANE-1,2-DIOL'>FEH</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=3wlf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wlf OCA], [https://pdbe.org/3wlf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wlf RCSB], [https://www.ebi.ac.uk/pdbsum/3wlf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wlf 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.


Authors: Wang, S.S., Nie, Y., Xu, Y., Zhang, R.Z., Huang, C.H., Chan, H.C., Guo, R.T. , Xiao, R.
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>


Description: Complex structure of RCR with (R)-PED
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wlf" 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]]
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