5k7p

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(New page: '''Unreleased structure''' The entry 5k7p is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (13:04, 1 March 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 5k7p is ON HOLD
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==MicroED structure of xylanase at 2.3 A resolution==
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<StructureSection load='5k7p' size='340' side='right'caption='[[5k7p]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5k7p]] 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=5K7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K7P FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2.3&#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=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=5k7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k7p OCA], [https://pdbe.org/5k7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k7p RCSB], [https://www.ebi.ac.uk/pdbsum/5k7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k7p 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: Cascio D]]
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[[Category: Eisenberg D]]
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[[Category: Gonen T]]
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[[Category: Hattne J]]
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[[Category: Reyes FE]]
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[[Category: Rodriguez J]]
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[[Category: Sawaya MR]]
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[[Category: Seidler P]]
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[[Category: Shi D]]
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[[Category: De la Cruz MJ]]

Current revision

MicroED structure of xylanase at 2.3 A resolution

PDB ID 5k7p

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