4e13: Difference between revisions
New page: '''Unreleased structure''' The entry 4e13 is ON HOLD Authors: Lu, M., White, M.A., Huang, Y., Wu, X., Liu, N., Cheng, X., Chen, Y. Description: Substrate-directed dual catalysis of dic... |
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==Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase== | |||
<StructureSection load='4e13' size='340' side='right'caption='[[4e13]], [[Resolution|resolution]] 2.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4e13]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi Acinetobacter baylyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E13 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E13 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]] 2.08Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4e13 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e13 OCA], [https://pdbe.org/4e13 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e13 RCSB], [https://www.ebi.ac.uk/pdbsum/4e13 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e13 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B1P3E1_ACIBI B1P3E1_ACIBI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Diketoreductase catalyzes a two-step bioreduction on a dicarbonyl substrate through a novel dual catalysis mode, in which random hydride attack simultaneously forms two mono-carbonyl intermediates, and subsequently distinct catalytic sites are responsible for the reductions of respective carbonyl group of the intermediates to yield the final dihydroxy product. | |||
Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase.,Lu M, Huang Y, White MA, Wu X, Liu N, Cheng X, Chen Y Chem Commun (Camb). 2012 Oct 24;48(92):11352-4. doi: 10.1039/c2cc36334h. PMID:23073461<ref>PMID:23073461</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4e13" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acinetobacter baylyi]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen Y]] | |||
[[Category: Cheng X]] | |||
[[Category: Huang Y]] | |||
[[Category: Liu N]] | |||
[[Category: Lu M]] | |||
[[Category: White MA]] | |||
[[Category: Wu X]] | |||