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[[Image:1ree.png|left|200px]]


{{STRUCTURE_1ree|  PDB=1ree  |  SCENE=  }}
==ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE==
 
<StructureSection load='1ree' size='340' side='right'caption='[[1ree]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
===ENDO-1,4-BETA-XYLANASE II COMPLEX WITH 3,4-EPOXYBUTYL-BETA-D-XYLOSIDE===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1ree]] is a 2 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=1REE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1REE FirstGlance]. <br>
{{ABSTRACT_PUBMED_8755744}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=07E:(3S)-3-hydroxybutyl+beta-D-xylopyranoside'>07E</scene>, <scene name='pdbligand=BEZ:BENZOIC+ACID'>BEZ</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ree FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ree OCA], [https://pdbe.org/1ree PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ree RCSB], [https://www.ebi.ac.uk/pdbsum/1ree PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ree ProSAT]</span></td></tr>
[[1ree]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REE OCA].  
</table>
 
== Function ==
==Reference==
[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>
<ref group="xtra">PMID:008755744</ref><references group="xtra"/>
== Evolutionary Conservation ==
[[Category: Endo-1,4-beta-xylanase]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/1ree_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ree ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trichoderma reesei]]
[[Category: Trichoderma reesei]]
[[Category: Havukainen, R.]]
[[Category: Havukainen R]]
[[Category: Rouvinen, J.]]
[[Category: Rouvinen J]]
[[Category: Torronen, A.]]
[[Category: Torronen A]]
[[Category: Hydrolase]]
[[Category: Xylan degradation]]
[[Category: Xylanase]]