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1jjb

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[[Image:1jjb.png|left|200px]]
 
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{{STRUCTURE_1jjb| PDB=1jjb | SCENE= }}
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==A neutral molecule in cation-binding site: Specific binding of PEG-SH to Acetylcholinesterase from Torpedo californica==
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<StructureSection load='1jjb' size='340' side='right'caption='[[1jjb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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===A neutral molecule in cation-binding site: Specific binding of PEG-SH to Acetylcholinesterase from Torpedo californica===
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jjb]] 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=1JJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JJB FirstGlance]. <br>
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{{ABSTRACT_PUBMED_12095250}}
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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]] 2.3&#8491;</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PE7:1-DEOXY-1-THIO-HEPTAETHYLENE+GLYCOL'>PE7</scene></td></tr>
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==About this Structure==
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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=1jjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjb OCA], [https://pdbe.org/1jjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jjb RCSB], [https://www.ebi.ac.uk/pdbsum/1jjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjb ProSAT]</span></td></tr>
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[[1jjb]] 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=1JJB OCA].
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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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/1jjb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1jjb ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
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*[[AChE bivalent inhibitors (Part II)|AChE bivalent inhibitors (Part II)]]
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*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
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*[[Acetylcholinesterase|Acetylcholinesterase]]
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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<ref group="xtra">PMID:012095250</ref><references group="xtra"/>
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[[Category: Tetronarce californica]]
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[[Category: Acetylcholinesterase]]
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[[Category: Koellner G]]
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[[Category: Torpedo californica]]
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[[Category: Millard CB]]
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[[Category: Koellner, G.]]
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[[Category: Silman I]]
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[[Category: Millard, C B.]]
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[[Category: Steiner T]]
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[[Category: Silman, I.]]
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[[Category: Sussman JL]]
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[[Category: Steiner, T.]]
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[[Category: Sussman, J L.]]
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[[Category: Alpha/beta hydrolase]]
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[[Category: Catalytic triad]]
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[[Category: Glycosylated protein]]
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[[Category: Hydrolase]]
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[[Category: Neurotransmitter cleavage]]
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[[Category: Serine hydrolase]]
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Current revision

A neutral molecule in cation-binding site: Specific binding of PEG-SH to Acetylcholinesterase from Torpedo californica

PDB ID 1jjb

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