5fcz: Difference between revisions
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==Streptomyces plicatus N-acetyl-beta-hexosaminidase in complex with Thio-NAglucal (TNX)== | |||
<StructureSection load='5fcz' size='340' side='right' caption='[[5fcz]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fcz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FCZ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TNX:N-[(2R,3S,4R)-2-(HYDROXYMETHYL)-3,4-BIS(OXIDANYL)-3,4-DIHYDRO-2H-PYRAN-5-YL]ETHANETHIOAMIDE'>TNX</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hp4|1hp4]], [[1hp5|1hp5]], [[1jak|1jak]], [[1m01|1m01]], [[5fd0|5fd0]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fcz OCA], [http://pdbe.org/5fcz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fcz RCSB], [http://www.ebi.ac.uk/pdbsum/5fcz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fcz ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mono-, di- and trisaccharide derivatives of 1,2-unsaturated N-acetyl-d-glucal have been synthesized and shown to function as tight-binding inhibitors/slow substrates of representative hexosaminidases. Turnover is slow and not observed in the thioamide analogue, allowing determination of the 3-dimensional structure of the complex. Inhibition is insensitive to pH and to mutation of key catalytic residues, consistent with the uncharged character of the inhibitor. These properties could render this inhibitor class less prone to development of resistance. | |||
N-Acetyl glycals are tight-binding and environmentally insensitive inhibitors of hexosaminidases.,Santana AG, Vadlamani G, Mark BL, Withers SG Chem Commun (Camb). 2016 Jun 28;52(51):7943-6. doi: 10.1039/c6cc02520j. Epub 2016, Jun 2. PMID:27253678<ref>PMID:27253678</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5fcz" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mark, B L]] | |||
[[Category: Vadlamani, G]] | |||
[[Category: Family 20 glycoside hydrolase]] | |||
[[Category: Gh20]] | |||
[[Category: Glycosidase inhibitor]] | |||
[[Category: Hexosaminidase]] | |||
[[Category: Hydrolase]] | |||
[[Category: Sphex]] | |||
[[Category: Thio-nag-glucal]] | |||
Revision as of 18:32, 26 October 2016
Streptomyces plicatus N-acetyl-beta-hexosaminidase in complex with Thio-NAglucal (TNX)
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