View source for 4qx4


==Human Aldose Reductase complexed with a ligand with a new scaffold at 1.26 A==
<StructureSection load='4qx4' size='340' side='right'caption='[[4qx4]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qx4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QX4 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]] 1.259&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3E2:(3-THIOXO-2,3-DIHYDRO-5H-[1,2,4]TRIAZINO[5,6-B]INDOL-5-YL)ACETIC+ACID'>3E2</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=4qx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qx4 OCA], [https://pdbe.org/4qx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qx4 RCSB], [https://www.ebi.ac.uk/pdbsum/4qx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qx4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fifteen compounds, sharing an indole-1-acetic acid moiety as a common fragment, were selected from commercial databases for testing aldose reductase inhibition. 3-Mercapto-5H-1,2,4-triazino[5,6-b]indole-5-acetic acid (13) was the most promising inhibitor, with an IC50 in the submicromolar range and high selectivity, relative to aldehyde reductase. The crystal structure of aldose reductase complexed with 13 revealed an interaction pattern explaining its high affinity. Physicochemical parameters underline the excellent "leadlikeness" of 13 as a promising candidate for further structure optimizations.

Identification of novel aldose reductase inhibitors based on carboxymethylated mercaptotriazinoindole scaffold.,Stefek M, Soltesova Prnova M, Majekova M, Rechlin C, Heine A, Klebe G J Med Chem. 2015 Mar 26;58(6):2649-57. doi: 10.1021/jm5015814. Epub 2015 Mar 4. PMID:25695864<ref>PMID:25695864</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qx4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Heine A]]
[[Category: Klebe G]]
[[Category: Rechlin C]]