4xv0: Difference between revisions
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<StructureSection load='4xv0' size='340' side='right'caption='[[4xv0]], [[Resolution|resolution]] 1.97Å' scene=''> | <StructureSection load='4xv0' size='340' side='right'caption='[[4xv0]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xv0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xv0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei_QM6a Trichoderma reesei QM6a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XV0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9697Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xv0 OCA], [https://pdbe.org/4xv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xv0 RCSB], [https://www.ebi.ac.uk/pdbsum/4xv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xv0 ProSAT]</span></td></tr> | |||
< | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/XYN3_HYPJQ XYN3_HYPJQ] 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. Produces xylobiose and xylotriose as the main degradation products.[UniProtKB:Q9P973] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cui | [[Category: Trichoderma reesei QM6a]] | ||
[[Category: Savchenko | [[Category: Cui H]] | ||
[[Category: Stogios | [[Category: Savchenko A]] | ||
[[Category: Xu | [[Category: Stogios PJ]] | ||
[[Category: Xu X]] | |||
Latest revision as of 10:50, 27 September 2023
Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from Trichoderma reeseiCrystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from Trichoderma reesei
Structural highlights
FunctionXYN3_HYPJQ 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. Produces xylobiose and xylotriose as the main degradation products.[UniProtKB:Q9P973] |
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