View source for 5zf3


==Crystal Structures of Endo-beta-1,4-xylanase II Complexed with Xylotriose==
<StructureSection load='5zf3' size='340' side='right'caption='[[5zf3]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zf3]] 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=5ZF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZF3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PRD_900117:4beta-beta-xylotriose'>PRD_900117</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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=5zf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zf3 OCA], [https://pdbe.org/5zf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zf3 RCSB], [https://www.ebi.ac.uk/pdbsum/5zf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zf3 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/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Trichoderma reesei RUT C-30]]
[[Category: Li Z]]
[[Category: Wan Q]]
[[Category: Zhang X]]