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4ey5

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==Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine A==
==Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine A==
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<StructureSection load='4ey5' size='340' side='right' caption='[[4ey5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='4ey5' size='340' side='right'caption='[[4ey5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ey5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EY5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EY5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ey5]] 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=4EY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EY5 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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HUP:HUPERZINE+A'>HUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HUP:HUPERZINE+A'>HUP</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACHE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4ey5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey5 OCA], [https://pdbe.org/4ey5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ey5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ey5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey5 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ey5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ey5 OCA], [http://pdbe.org/4ey5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ey5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ey5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ey5 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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==See Also==
==See Also==
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
 
== 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: Human]]
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[[Category: Large Structures]]
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[[Category: Burshteyn, F]]
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[[Category: Burshteyn F]]
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[[Category: Cassidy, M]]
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[[Category: Cassidy M]]
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[[Category: Cheung, J]]
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[[Category: Cheung J]]
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[[Category: Franklin, M]]
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[[Category: Franklin M]]
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[[Category: Gary, E]]
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[[Category: Gary E]]
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[[Category: Height, J]]
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[[Category: Height J]]
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[[Category: Love, J]]
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[[Category: Love J]]
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[[Category: Rudolph, M]]
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[[Category: Rudolph M]]
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[[Category: Huperzine some]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Inhibitor]]
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Revision as of 04:22, 7 October 2022

Crystal Structure of Recombinant Human Acetylcholinesterase in Complex with (-)-huperzine A

PDB ID 4ey5

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