7mgu
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Improved ligand discovery using micro-beam data collection at the edge of protein crystals== | ==Improved ligand discovery using micro-beam data collection at the edge of protein crystals== | ||
| - | <StructureSection load='7mgu' size='340' side='right'caption='[[7mgu]]' scene=''> | + | <StructureSection load='7mgu' size='340' side='right'caption='[[7mgu]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MGU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7mgu]] 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=7MGU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MGU FirstGlance]. <br> |
| - | </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=7mgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mgu OCA], [https://pdbe.org/7mgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mgu RCSB], [https://www.ebi.ac.uk/pdbsum/7mgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mgu ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=7mgu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mgu OCA], [https://pdbe.org/7mgu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mgu RCSB], [https://www.ebi.ac.uk/pdbsum/7mgu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mgu ProSAT]</span></td></tr> | ||
</table> | </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__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Trichoderma reesei]] | ||
[[Category: Jakoncic J]] | [[Category: Jakoncic J]] | ||
[[Category: Soares AS]] | [[Category: Soares AS]] | ||
Revision as of 16:11, 18 October 2023
Improved ligand discovery using micro-beam data collection at the edge of protein crystals
| |||||||||||
