6idw: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 6idw is ON HOLD
+==GH6 Orpinomyces sp. Y102 enzyme==
+<StructureSection load='6idw' size='340' side='right'caption='[[6idw]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6idw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Orpinomyces_sp._Y102 Orpinomyces sp. Y102]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5jx6 5jx6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IDW 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]] 2.78&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</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=6idw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6idw OCA], [https://pdbe.org/6idw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6idw RCSB], [https://www.ebi.ac.uk/pdbsum/6idw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6idw ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A076U926_9FUNG A0A076U926_9FUNG]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The catalytic domain (residues 128-449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 A, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.
-Authors: Tsai, L.C., Huang, H.C.
+Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose.,Huang HC, Qi LH, Chen YC, Tsai LC Acta Crystallogr D Struct Biol. 2019 Dec 1;75(Pt 12):1138-1147. doi:, 10.1107/S2059798319013597. Epub 2019 Nov 29. PMID:31793907<ref>PMID:31793907</ref>
-Description: GH6 Orpinomyces sp. Y102 enzyme
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Tsai, L.C]]
+<div class="pdbe-citations 6idw" style="background-color:#fffaf0;"></div>
-[[Category: Huang, H.C]]
+==See Also==
+*[[Glucanase 3D structures|Glucanase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Orpinomyces sp. Y102]]
+[[Category: Huang HC]]
+[[Category: Tsai LC]]