1ku6: Difference between revisions

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OCA

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 ==Fasciculin 2-Mouse Acetylcholinesterase Complex==
-<StructureSection load='1ku6' size='340' side='right' caption='[[1ku6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='1ku6' size='340' side='right'caption='[[1ku6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ku6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KU6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ku6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dendroaspis_angusticeps Dendroaspis angusticeps] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KU6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.5&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mah|1mah]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1ku6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ku6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ku6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ku6 PDBsum]</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=1ku6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ku6 OCA], [https://pdbe.org/1ku6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ku6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ku6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ku6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/1ku6_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ku/1ku6_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </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=1ku6 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 27: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ku6" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Acetylcholinesterase|Acetylcholinesterase]]
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
 *[[Fasciculin|Fasciculin]]
 == References ==
@@ Line 36: / Line 38: @@
 </StructureSection>
 [[Category: Dendroaspis angusticeps]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Bourne, Y]]
+[[Category: Bourne Y]]
-[[Category: Burmeister, W]]
+[[Category: Burmeister W]]
-[[Category: Marchot, P]]
+[[Category: Marchot P]]
-[[Category: Taylor, P]]
+[[Category: Taylor P]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-toxin complex]]
-[[Category: Serine esterase]]
-[[Category: Synapse]]
-[[Category: Toxin]]
-[[Category: Venom]]