5zo0

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(New page: '''Unreleased structure''' The entry 5zo0 is ON HOLD Authors: Wan, Q., Li, Z.H. Description: neutron structure of xylanase at pD5.4 Category: Unreleased Structures [[Category: Wan,...)
Current revision (09:01, 22 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5zo0 is ON HOLD
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==Neutron structure of xylanase at pD5.4==
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<StructureSection load='5zo0' size='340' side='right'caption='[[5zo0]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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Authors: Wan, Q., Li, Z.H.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5zo0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei_RUT_C-30 Trichoderma reesei RUT C-30]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZO0 FirstGlance]. <br>
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Description: neutron structure of xylanase at pD5.4
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 1.648&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene></td></tr>
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[[Category: Wan, Q]]
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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=5zo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zo0 OCA], [https://pdbe.org/5zo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zo0 RCSB], [https://www.ebi.ac.uk/pdbsum/5zo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zo0 ProSAT]</span></td></tr>
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[[Category: Li, Z.H]]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/XYN2_HYPJR XYN2_HYPJR] Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose (PubMed:1369024, Ref.5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747).<ref>PMID:1369024</ref> <ref>PMID:19556747</ref> <ref>PMID:7988708</ref> <ref>PMID:1369024</ref>
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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: Trichoderma reesei RUT C-30]]
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[[Category: Li ZH]]
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[[Category: Wan Q]]

Current revision

Neutron structure of xylanase at pD5.4

PDB ID 5zo0

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