6o66: Difference between revisions
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==Structure of VX-phosphonylated hAChE in complex with oxime reactivator RS-170B== | |||
<StructureSection load='6o66' size='340' side='right'caption='[[6o66]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6o66]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O66 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LND:4-carbamoyl-1-(3-{2-[(E)-(hydroxyimino)methyl]-1H-imidazol-1-yl}propyl)pyridin-1-ium'>LND</scene></td></tr> | |||
[[Category: | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SVX:O-[(R)-ETHOXY(METHYL)PHOSPHORYL]-L-SERINE'>SVX</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6o5r|6o5r]], [[6o5s|6o5s]], [[6o5v|6o5v]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span></td></tr> | |||
<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=6o66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o66 OCA], [http://pdbe.org/6o66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o66 RCSB], [http://www.ebi.ac.uk/pdbsum/6o66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o66 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/ACES_HUMAN ACES_HUMAN]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis.<ref>PMID:2714437</ref> <ref>PMID:1748670</ref> <ref>PMID:1517212</ref> <ref>PMID:11985878</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Acetylcholinesterase]] | |||
[[Category: Large Structures]] | |||
[[Category: Gerlits, O]] | [[Category: Gerlits, O]] | ||
[[Category: Kovalevsky, A]] | |||
[[Category: Radic, Z]] | [[Category: Radic, Z]] | ||
[[Category: | [[Category: Human acetylcholinesterase]] | ||
[[Category: Hydrolase]] | |||
[[Category: Imidazole-based oxime]] | |||
[[Category: Oxime reactivator]] | |||
[[Category: Rs-170b]] | |||
[[Category: Vx-hache]] | |||
[[Category: Vx-phosphonylated]] | |||
Revision as of 06:16, 29 May 2019
Structure of VX-phosphonylated hAChE in complex with oxime reactivator RS-170B
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