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2ha0
From Proteopedia
(Difference between revisions)
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==Crystal structure of mouse acetylcholinesterase complexed with 4-ketoamyltrimethylammonium== | ==Crystal structure of mouse acetylcholinesterase complexed with 4-ketoamyltrimethylammonium== | ||
| - | <StructureSection load='2ha0' size='340' side='right' caption='[[2ha0]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='2ha0' size='340' side='right'caption='[[2ha0]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ha0]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ha0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HA0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CHH:N,N,N-TRIMETHYL-4-OXOPENTAN-1-AMINIUM'>CHH</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NWA:4,4-DIHYDROXY-N,N,N-TRIMETHYLPENTAN-1-AMINIUM'>NWA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHH:N,N,N-TRIMETHYL-4-OXOPENTAN-1-AMINIUM'>CHH</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NWA:4,4-DIHYDROXY-N,N,N-TRIMETHYLPENTAN-1-AMINIUM'>NWA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1j06|1j06]], [[2h9y|2h9y]], [[2ha2|2ha2]], [[2ha3|2ha3]], [[2ha4|2ha4]], [[2ha5|2ha5]], [[2ha6|2ha6]], [[2ha7|2ha7]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1j06|1j06]], [[2h9y|2h9y]], [[2ha2|2ha2]], [[2ha3|2ha3]], [[2ha4|2ha4]], [[2ha5|2ha5]], [[2ha6|2ha6]], [[2ha7|2ha7]]</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/Acetylcholinesterase Acetylcholinesterase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ha0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ha0 OCA], [https://pdbe.org/2ha0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ha0 RCSB], [https://www.ebi.ac.uk/pdbsum/2ha0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ha0 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ACES_MOUSE ACES_MOUSE]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ha/2ha0_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ha/2ha0_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
| - | *[[3D structures | + | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Bourne, Y]] | [[Category: Bourne, Y]] | ||
Revision as of 17:26, 10 March 2021
Crystal structure of mouse acetylcholinesterase complexed with 4-ketoamyltrimethylammonium
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