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==NATIVE MONOCLINIC FORM OF TORPEDO ACETYLCHOLINESTERASE==
 
<StructureSection load='2j3d' size='340' side='right' caption='[[2j3d]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
==Native monoclinic form of Torpedo acetylcholinesterase==
<StructureSection load='2j3d' size='340' side='right'caption='[[2j3d]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2j3d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J3D FirstGlance]. <br>
<table><tr><td colspan='2'>[[2j3d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J3D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1acj|1acj]], [[1acl|1acl]], [[1amn|1amn]], [[1ax9|1ax9]], [[1cfj|1cfj]], [[1dx6|1dx6]], [[1e3q|1e3q]], [[1e66|1e66]], [[1ea5|1ea5]], [[1eea|1eea]], [[1eve|1eve]], [[1fss|1fss]], [[1gpk|1gpk]], [[1gpn|1gpn]], [[1gqr|1gqr]], [[1gqs|1gqs]], [[1h22|1h22]], [[1h23|1h23]], [[1hbj|1hbj]], [[1jga|1jga]], [[1jgb|1jgb]], [[1jjb|1jjb]], [[1oce|1oce]], [[1odc|1odc]], [[1qid|1qid]], [[1qie|1qie]], [[1qif|1qif]], [[1qig|1qig]], [[1qih|1qih]], [[1qii|1qii]], [[1qij|1qij]], [[1qik|1qik]], [[1qim|1qim]], [[1qti|1qti]], [[1som|1som]], [[1u65|1u65]], [[1ut6|1ut6]], [[1vot|1vot]], [[1vxo|1vxo]], [[1vxr|1vxr]], [[1w4l|1w4l]], [[1w6r|1w6r]], [[1w75|1w75]], [[1w76|1w76]], [[1zgb|1zgb]], [[1zgc|1zgc]], [[2ace|2ace]], [[2ack|2ack]], [[2c4h|2c4h]], [[2c58|2c58]], [[2c5f|2c5f]], [[2c5g|2c5g]], [[2cek|2cek]], [[2ckm|2ckm]], [[2cmf|2cmf]], [[2dfp|2dfp]], [[3ace|3ace]], [[4ace|4ace]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2j3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3d OCA], [https://pdbe.org/2j3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j3d RCSB], [https://www.ebi.ac.uk/pdbsum/2j3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j3d ProSAT]</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=2j3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j3d OCA], [http://pdbe.org/2j3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j3d RCSB], [http://www.ebi.ac.uk/pdbsum/2j3d PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ACES_TORCA ACES_TORCA]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.  
[https://www.uniprot.org/uniprot/ACES_TETCF ACES_TETCF] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
== 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/j3/2j3d_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j3/2j3d_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>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j3d ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Acetylcholinesterase|Acetylcholinesterase]]
*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acetylcholinesterase]]
[[Category: Large Structures]]
[[Category: Harel, M]]
[[Category: Tetronarce californica]]
[[Category: Sussman, J L]]
[[Category: Harel M]]
[[Category: Alzheimer's disease]]
[[Category: Sussman JL]]
[[Category: Cholinesterase]]
[[Category: Glycoprotein]]
[[Category: Gpi-anchor]]
[[Category: Hydrolase]]
[[Category: Lipoprotein]]
[[Category: Membrane]]
[[Category: Muscle]]
[[Category: Nerve]]
[[Category: Neurotransmitter degradation]]
[[Category: Serine esterase]]
[[Category: Serine hydrolase]]
[[Category: Synapse]]

Latest revision as of 17:33, 13 December 2023

Native monoclinic form of Torpedo acetylcholinesteraseNative monoclinic form of Torpedo acetylcholinesterase

Structural highlights

2j3d is a 1 chain structure with sequence from Tetronarce californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACES_TETCF Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2j3d, resolution 2.60Å

Drag the structure with the mouse to rotate

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OCA
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