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6cqv

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==Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with VX(+) and HI-6==
==Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with VX(+) and HI-6==
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<StructureSection load='6cqv' size='340' side='right' caption='[[6cqv]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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<StructureSection load='6cqv' size='340' side='right'caption='[[6cqv]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6cqv]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CQV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6cqv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CQV 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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HI6:4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM'>HI6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=VX:O-ETHYLMETHYLPHOSPHONIC+ACID+ESTER+GROUP'>VX</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]] 2.601&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cqt|6cqt]], [[6cqu|6cqu]], [[6cqw|6cqw]], [[6cqx|6cqx]], [[6cqy|6cqy]], [[6cqz|6cqz]]</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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HI6:4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM'>HI6</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=VX:O-ETHYLMETHYLPHOSPHONIC+ACID+ESTER+GROUP'>VX</scene></td></tr>
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<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>
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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=6cqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cqv OCA], [https://pdbe.org/6cqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cqv RCSB], [https://www.ebi.ac.uk/pdbsum/6cqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cqv ProSAT]</span></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=6cqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cqv OCA], [http://pdbe.org/6cqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cqv RCSB], [http://www.ebi.ac.uk/pdbsum/6cqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cqv ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[https://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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6cqv" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6cqv" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetylcholinesterase]]
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[[Category: Homo sapiens]]
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[[Category: Bester, S M]]
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[[Category: Large Structures]]
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[[Category: Guelta, M A]]
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[[Category: Bester SM]]
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[[Category: Height, J J]]
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[[Category: Guelta MA]]
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[[Category: Pegan, S D]]
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[[Category: Height JJ]]
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[[Category: Hydrolase]]
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[[Category: Pegan SD]]

Current revision

Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with VX(+) and HI-6

PDB ID 6cqv

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