3rx5

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<StructureSection load='3rx5' size='340' side='right'caption='[[3rx5]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='3rx5' size='340' side='right'caption='[[3rx5]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rx5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliac Aliac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RX5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rx5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius_subsp._acidocaldarius Alicyclobacillus acidocaldarius subsp. acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RX5 FirstGlance]. <br>
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</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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G2I:(3R,4R,5R)-3-HYDROXY-5-(HYDROXYMETHYL)PIPERIDIN-4-YL+4-O-BETA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE'>G2I</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.99&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gzk|3gzk]], [[3h2w|3h2w]], [[3h3k|3h3k]], [[3rx7|3rx7]], [[3rx8|3rx8]]</div></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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G2I:(3R,4R,5R)-3-HYDROXY-5-(HYDROXYMETHYL)PIPERIDIN-4-YL+4-O-BETA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE'>G2I</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">celA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1388 ALIAC])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=3rx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rx5 OCA], [https://pdbe.org/3rx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rx5 RCSB], [https://www.ebi.ac.uk/pdbsum/3rx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rx5 ProSAT]</span></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=3rx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rx5 OCA], [https://pdbe.org/3rx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rx5 RCSB], [https://www.ebi.ac.uk/pdbsum/3rx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rx5 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q9AJS0_ALIAC Q9AJS0_ALIAC]
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Using structural insight, the binding mode of isofagomine-derived inhibitors with family GH9 glycosidases is achieved via the study of Alicyclobacillus acidocaldarius (AaCel9A) endoglucanase. In contrast to what was observed in the first report using these compounds with inverting glycosidases from family GH6, these inhibitors do not adopt a distorted conformation in the active site.
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A potential fortuitous binding of inhibitors of an inverting family GH9 beta-glycosidase derived from isofagomine.,Morera S, Vigouroux A, Stubbs KA Org Biomol Chem. 2011 Sep 7;9(17):5945-7. Epub 2011 Jul 25. PMID:21785782<ref>PMID:21785782</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 3rx5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aliac]]
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[[Category: Alicyclobacillus acidocaldarius subsp. acidocaldarius]]
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[[Category: Cellulase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Morera, S]]
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[[Category: Morera S]]
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[[Category: Vigouroux, A]]
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[[Category: Vigouroux A]]
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[[Category: Endoglucanase]]
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[[Category: Gh9 family fold]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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Current revision

structure of AaCel9A in complex with cellotriose-like isofagomine

PDB ID 3rx5

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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