5h9y

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'''Unreleased structure'''
 
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The entry 5h9y is ON HOLD until Dec 29 2017
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==Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose.==
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<StructureSection load='5h9y' size='340' side='right'caption='[[5h9y]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5h9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_barengoltzii Paenibacillus barengoltzii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H9Y FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.969&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5h9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h9y OCA], [https://pdbe.org/5h9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h9y RCSB], [https://www.ebi.ac.uk/pdbsum/5h9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h9y ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A1S4NYE2_9BACL A0A1S4NYE2_9BACL]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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beta-1,3-Glucan is one of the most abundant polysaccharides in fungi. Recognition of beta-1,3-glucan occurs in both hydrolysis by glycoside hydrolases and immunological recognition. Our study provides a novel structural account of how glycoside hydrolase recognizes and hydrolyzes substrates in a triple-helical form and presents a general structural basis of beta-1,3-glucan recognition.
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Authors: Zhen, Q., Yan, Q., Yang, S., Jiang, Z., You, X.
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The recognition mechanism of triple-helical beta-1,3-glucan by a beta-1,3-glucanase.,Qin Z, Yang D, You X, Liu Y, Hu S, Yan Q, Yang S, Jiang Z Chem Commun (Camb). 2017 Aug 17;53(67):9368-9371. doi: 10.1039/c7cc03330c. PMID:28787048<ref>PMID:28787048</ref>
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Description: Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Zhen, Q]]
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<div class="pdbe-citations 5h9y" style="background-color:#fffaf0;"></div>
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[[Category: Jiang, Z]]
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[[Category: You, X]]
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==See Also==
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[[Category: Yang, S]]
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*[[Glucanase 3D structures|Glucanase 3D structures]]
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[[Category: Yan, Q]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Paenibacillus barengoltzii]]
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[[Category: Jiang Z]]
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[[Category: Yan Q]]
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[[Category: Yang S]]
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[[Category: You X]]
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[[Category: Zhen Q]]

Current revision

Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose.

PDB ID 5h9y

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