5k7p
From Proteopedia
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(New page: '''Unreleased structure''' The entry 5k7p is ON HOLD Authors: Description: Category: Unreleased Structures) |
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- | '''Unreleased structure''' | ||
- | + | ==MicroED structure of xylanase at 2.3 A resolution== | |
- | + | <StructureSection load='5k7p' size='340' side='right'caption='[[5k7p]], [[Resolution|resolution]] 2.30Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <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> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 2.3Å</td></tr> | |
- | [[Category: | + | <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> |
+ | <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> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [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> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Trichoderma reesei]] | ||
+ | [[Category: Cascio D]] | ||
+ | [[Category: Eisenberg D]] | ||
+ | [[Category: Gonen T]] | ||
+ | [[Category: Hattne J]] | ||
+ | [[Category: Reyes FE]] | ||
+ | [[Category: Rodriguez J]] | ||
+ | [[Category: Sawaya MR]] | ||
+ | [[Category: Seidler P]] | ||
+ | [[Category: Shi D]] | ||
+ | [[Category: De la Cruz MJ]] |
Current revision
MicroED structure of xylanase at 2.3 A resolution
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Categories: Large Structures | Trichoderma reesei | Cascio D | Eisenberg D | Gonen T | Hattne J | Reyes FE | Rodriguez J | Sawaya MR | Seidler P | Shi D | De la Cruz MJ