5m77
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==a GH76 family enzyme structure== | |
| + | <StructureSection load='5m77' size='340' side='right' caption='[[5m77]], [[Resolution|resolution]] 1.46Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m77]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M77 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7K2:(2~{R},3~{S},4~{S},5~{S},6~{R})-2-[[(3~{S},4~{R},5~{R})-4,5-bis(oxidanyl)piperidin-3-yl]methylsulfanyl]-6-(hydroxymethyl)oxane-3,4,5-triol'>7K2</scene>, <scene name='pdbligand=7K3:(2~{R},3~{S},4~{S},5~{S},6~{R})-2-(hydroxymethyl)-6-sulfanyl-oxane-3,4,5-triol'>7K3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=5m77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m77 OCA], [http://pdbe.org/5m77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m77 RCSB], [http://www.ebi.ac.uk/pdbsum/5m77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m77 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The non-hydrolyzable S-linked azasugars, 1,6-alpha-mannosylthio- and 1,6-alpha-mannobiosylthioisofagomine, were synthesized and shown to bind with high affinity to a family 76 endo-1,6-alpha-mannanase from Bacillus circulans. X-ray crystallography showed an atypical interaction of the isofagomine nitrogen with the catalytic acid/base. Molecular dynamics simulations reveal that the atypical binding results from sulfur perturbing the most stable form away from the nucleophile interaction preferred for the O-linked congener. | ||
| - | + | An atypical interaction explains the high-affinity of a non-hydrolyzable S-linked 1,6-alpha-mannanase inhibitor.,Belz T, Jin Y, Coines J, Rovira C, Davies GJ, Williams SJ Chem Commun (Camb). 2017 Aug 25;53(66):9238-9241. doi: 10.1039/c7cc04977c. Epub, 2017 Aug 2. PMID:28766587<ref>PMID:28766587</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5m77" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Davies, G]] | ||
| + | [[Category: Jin, Y]] | ||
| + | [[Category: Williams, S]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Glycoside hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Mannanase]] | ||
| + | [[Category: S-linked polysaccharide]] | ||
Revision as of 05:56, 17 August 2017
a GH76 family enzyme structure
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