5fd0
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Streptomyces plicatus N-acetyl-beta-hexosaminidase in complex with NAGlucal== | |
| + | <StructureSection load='5fd0' size='340' side='right' caption='[[5fd0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5fd0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FD0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]], [[5fcz|5fcz]]</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=5fd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fd0 OCA], [http://pdbe.org/5fd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fd0 RCSB], [http://www.ebi.ac.uk/pdbsum/5fd0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fd0 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 5fd0" 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: Nag-glucal]] | ||
| + | [[Category: Sphex]] | ||
Revision as of 18:27, 26 October 2016
Streptomyces plicatus N-acetyl-beta-hexosaminidase in complex with NAGlucal
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