4hko

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'''Unreleased structure'''
 
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The entry 4hko is ON HOLD until Jan 20 2015
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==Crystal Structures of Mutant Endo-beta-1,4-xylanase II (E177Q) in the apo form==
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<StructureSection load='4hko' size='340' side='right'caption='[[4hko]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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Authors: Langan, P., Wan, Q., Coates, L., Kovalevsky, A.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4hko]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HKO FirstGlance]. <br>
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Description: Crystal Structures of Mutant Endo-beta-1,4-xylanase II (E177Q) in the apo form
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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]] 1.5&#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=IOD:IODIDE+ION'>IOD</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=4hko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hko OCA], [https://pdbe.org/4hko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hko RCSB], [https://www.ebi.ac.uk/pdbsum/4hko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hko ProSAT]</span></td></tr>
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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]]
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[[Category: Coates L]]
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[[Category: Kovalevsky A]]
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[[Category: Langan P]]
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[[Category: Wan Q]]

Current revision

Crystal Structures of Mutant Endo-beta-1,4-xylanase II (E177Q) in the apo form

PDB ID 4hko

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