3wnq: Difference between revisions
Jump to navigation
Jump to search
m Protected "3wnq" [edit=sysop:move=sysop] |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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]] 2.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wnq]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</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='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> | |||
== 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 3wnq" 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: Ko TP]] | |||
[[Category: Nie Y]] | |||
[[Category: Wang SS]] | |||
[[Category: Xiao R]] | |||
[[Category: Xu Y]] | |||
[[Category: Zhang RZ]] | |||
Latest revision as of 16:17, 8 November 2023
Crystal structure of (R)-carbonyl reductase H49A mutant from Candida Parapsilosis in complex with 2-hydroxyacetophenoneCrystal structure of (R)-carbonyl reductase H49A mutant from Candida Parapsilosis in complex with 2-hydroxyacetophenone
Structural highlights
FunctionPublication Abstract from PubMedStructure-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. See AlsoReferences
|
| ||||||||||||||||||