3zj7
From Proteopedia
(Difference between revisions)
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==Crystal structure of strictosidine glucosidase in complex with inhibitor-1== | ==Crystal structure of strictosidine glucosidase in complex with inhibitor-1== | ||
- | <StructureSection load='3zj7' size='340' side='right' caption='[[3zj7]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='3zj7' size='340' side='right'caption='[[3zj7]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3zj7]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3zj7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ophioxylon_serpentinum Ophioxylon serpentinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZJ7 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C1K:(1R,2S,3S,4R,5R)-4-(CYCLOHEXYLAMINO)-5-(HYDROXYMETHYL)CYCLOPENTANE-1,2,3-TRIOL'>C1K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1K:(1R,2S,3S,4R,5R)-4-(CYCLOHEXYLAMINO)-5-(HYDROXYMETHYL)CYCLOPENTANE-1,2,3-TRIOL'>C1K</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zj6|3zj6]], [[3zj8|3zj8]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zj6|3zj6]], [[3zj8|3zj8]]</div></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-alpha-(S)-strictosidine_beta-glucosidase 3-alpha-(S)-strictosidine beta-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.105 3.2.1.105] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zj7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zj7 OCA], [https://pdbe.org/3zj7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zj7 RCSB], [https://www.ebi.ac.uk/pdbsum/3zj7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zj7 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/SG1_RAUSE SG1_RAUSE]] Glucosidase specifically involved in alkaloid biosynthesis leading to the accumulation of several alkaloids, including ajmaline, an important plant-derived pharmaceutical used in the therapy of heart disorders.<ref>PMID:22004291</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
- | *[[Beta-glucosidase|Beta-glucosidase]] | + | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Ophioxylon serpentinum]] | [[Category: Ophioxylon serpentinum]] | ||
[[Category: Castiglia, A]] | [[Category: Castiglia, A]] |
Revision as of 05:48, 10 August 2022
Crystal structure of strictosidine glucosidase in complex with inhibitor-1
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Categories: Large Structures | Ophioxylon serpentinum | Castiglia, A | Jaeger, V | Lin, H | Panjikar, S | Rajendran, C | Ruppert, M | Schuebel, H | Stoeckigt, J | Wang, M | Warzecha, H | Xia, L | Ajmaline | Alkaloid | Hydrolase | Inhibitor