View source for 3sur


==Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline.==
<StructureSection load='3sur' size='340' side='right'caption='[[3sur]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sur]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_sp._TS12 Paenibacillus sp. TS12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SUR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SUR 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NGT:3AR,5R,6S,7R,7AR-5-HYDROXYMETHYL-2-METHYL-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D]THIAZOLE-6,7-DIOL'>NGT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3sur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sur OCA], [https://pdbe.org/3sur PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sur RCSB], [https://www.ebi.ac.uk/pdbsum/3sur PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sur ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D2KW09_9BACL D2KW09_9BACL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
One useful methodology that has been used to give insight into how chemically synthesized inhibitors bind to enzymes and the reasons underlying their potency is crystallographic studies of inhibitor-enzyme complexes. Presented here is the X-ray structural analysis of a representative family 20 exo-beta-N-acetylhexosaminidase in complex with various known classes of inhibitor of these types of enzymes, which highlights how different inhibitor classes can inhibit the same enzyme. This study will aid in the future development of inhibitors of not only exo-beta-N-acetylhexosaminidases but also other types of glycoside hydrolases.

Gaining insight into the inhibition of glycoside hydrolase family 20 exo-beta-N-acetylhexosaminidases using a structural approach.,Sumida T, Stubbs KA, Ito M, Yokoyama S Org Biomol Chem. 2012 Apr 7;10(13):2607-12. Epub 2012 Feb 27. PMID:22367352<ref>PMID:22367352</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3sur" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
*[[Beta-N-acetylhexosaminidase 3D structures|Beta-N-acetylhexosaminidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paenibacillus sp. TS12]]
[[Category: Sumida T]]
[[Category: Yokoyama S]]