6idw

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<StructureSection load='6idw' size='340' side='right'caption='[[6idw]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
<StructureSection load='6idw' size='340' side='right'caption='[[6idw]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6idw]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IDW FirstGlance]. <br>
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<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>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBI:CELLOBIOSE'>CBI</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></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]] 2.78&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cbhC7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=884017 Orpinomyces sp. Y102])</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=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>
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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=6idw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6idw OCA], [http://pdbe.org/6idw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6idw RCSB], [http://www.ebi.ac.uk/pdbsum/6idw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6idw ProSAT]</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=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>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A076U926_9FUNG A0A076U926_9FUNG]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6idw" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Glucanase 3D structures|Glucanase 3D structures]]
*[[Glucanase 3D structures|Glucanase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Orpinomyces sp. y102]]
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[[Category: Orpinomyces sp. Y102]]
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[[Category: Huang, H C]]
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[[Category: Huang HC]]
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[[Category: Tsai, L C]]
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[[Category: Tsai LC]]
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[[Category: Cbh7]]
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[[Category: Endoglucanase]]
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[[Category: Exoglucanase]]
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[[Category: Gh6]]
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[[Category: Hydrolase]]
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[[Category: Orpinomyces sp]]
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Current revision

GH6 Orpinomyces sp. Y102 enzyme

PDB ID 6idw

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