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5zh0

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Current revision (08:54, 22 November 2023) (edit) (undo)
 
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<StructureSection load='5zh0' size='340' side='right'caption='[[5zh0]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
<StructureSection load='5zh0' size='340' side='right'caption='[[5zh0]], [[Resolution|resolution]] 1.08&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zh0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZH0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zh0]] 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=5ZH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZH0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.08&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dfc|2dfc]], [[4hkw|4hkw]], [[4hki|4hki]], [[4hk9|4hk9]], [[4hko|4hko]]</td></tr>
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<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></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></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=5zh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zh0 OCA], [https://pdbe.org/5zh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zh0 RCSB], [https://www.ebi.ac.uk/pdbsum/5zh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zh0 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zh0 OCA], [http://pdbe.org/5zh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zh0 RCSB], [http://www.ebi.ac.uk/pdbsum/5zh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zh0 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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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[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 ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Endo-1,4-beta-xylanase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, Z]]
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[[Category: Trichoderma reesei RUT C-30]]
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[[Category: Wan, Q]]
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[[Category: Li Z]]
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[[Category: Zhang, X]]
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[[Category: Wan Q]]
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[[Category: Hydrolase]]
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[[Category: Zhang X]]
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[[Category: Xylanase ii]]
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Current revision

Crystal Structures of Endo-beta-1,4-xylanase II

PDB ID 5zh0

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