View source for 5m77


==a GH76 family enzyme structure==
<StructureSection load='5m77' size='340' side='right'caption='[[5m77]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5m77]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5M77 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]] 1.46&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7K2:[(3S,4R,5R)-4,5-dihydroxypiperidin-3-yl]methyl+1-thio-alpha-D-mannopyranoside'>7K2</scene>, <scene name='pdbligand=7K3:1-thio-alpha-D-mannopyranose'>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'>[https://proteopedia.org/fgij/fg.htm?mol=5m77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m77 OCA], [https://pdbe.org/5m77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m77 RCSB], [https://www.ebi.ac.uk/pdbsum/5m77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m77 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9Z4P9_NIACI Q9Z4P9_NIACI] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5m77" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Niallia circulans]]
[[Category: Davies G]]
[[Category: Jin Y]]
[[Category: Williams S]]