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1ut6

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==STRUCTURE OF ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH N-9-(1',2',3',4'-TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE AT 2.4 ANGSTROMS RESOLUTION.==
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<StructureSection load='1ut6' size='340' side='right' caption='[[1ut6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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==Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with N-9-(1',2',3',4'-Tetrahydroacridinyl)-1,8- diaminooctane at 2.4 angstroms resolution.==
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<StructureSection load='1ut6' size='340' side='right'caption='[[1ut6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ut6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UT6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UT6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ut6]] 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=1UT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UT6 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=A8N:N-9-(1,2,3,4-TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE'>A8N</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
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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]] 2.4&#8491;</td></tr>
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<tr><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]], [[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]], [[1vot|1vot]], [[1vxo|1vxo]], [[1vxr|1vxr]], [[2ace|2ace]], [[2ack|2ack]], [[2dfp|2dfp]], [[3ace|3ace]], [[4ace|4ace]]</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=A8N:N-9-(1,2,3,4-TETRAHYDROACRIDINYL)-1,8-DIAMINOOCTANE'>A8N</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr><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=1ut6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut6 OCA], [https://pdbe.org/1ut6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ut6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ut6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ut6 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ut6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ut6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ut6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ut6 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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[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>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ut/1ut6_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ut/1ut6_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>
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</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].
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</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=1ut6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 1ut6" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[AChE bivalent inhibitors|AChE bivalent inhibitors]]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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*[[Acetylcholinesterase|Acetylcholinesterase]]
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*[[Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane|Acetylcholinesterase complexed with N-9-(1'%2C2'%2C3'%2C4'-tetrahydroacridinyl)-1%2C8-diaminooctane]]
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*[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (5 carbon linker)]]
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*[[Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)|Torpedo californica acetylcholinesterase with alkylene-linked tacrine dimer (7 carbon linker)]]
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*[[User:Boris Brumshtein|User:Boris Brumshtein]]
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*[[User:Dawn M. Wong|User:Dawn M. Wong]]
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetylcholinesterase]]
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[[Category: Large Structures]]
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[[Category: Torpedo californica]]
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[[Category: Tetronarce californica]]
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[[Category: Brumshtein, B.]]
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[[Category: Brumshtein B]]
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[[Category: Carlier, P R.]]
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[[Category: Carlier PR]]
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[[Category: Greenblatt, H M.]]
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[[Category: Greenblatt HM]]
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[[Category: Pang, Y P.]]
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[[Category: Pang Y-P]]
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[[Category: Silman, I.]]
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[[Category: Silman I]]
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[[Category: Sussman, J L.]]
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[[Category: Sussman JL]]
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[[Category: Wong, D M.]]
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[[Category: Wong DM]]
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[[Category: Acetylcholinesterase]]
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[[Category: Alzheimer's disease]]
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[[Category: Amine]]
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[[Category: Bivalent ligand]]
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[[Category: Dual-site binding]]
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[[Category: Glycoprotein]]
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[[Category: Gpi-anchor neurotransmitter degradation]]
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[[Category: Heterodimer]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Membrane]]
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[[Category: Muscle]]
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[[Category: Nerve]]
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[[Category: Neurotransmitter cleavage]]
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[[Category: Serine esterase synapse]]
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[[Category: Serine hydrolase]]
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[[Category: Tacrine]]
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Current revision

Structure of acetylcholinesterase (E.C. 3.1.1.7) complexed with N-9-(1',2',3',4'-Tetrahydroacridinyl)-1,8- diaminooctane at 2.4 angstroms resolution.

PDB ID 1ut6

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