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1e66
From Proteopedia
(Difference between revisions)
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==STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE X AT 2.1A RESOLUTION== | ==STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE X AT 2.1A RESOLUTION== | ||
| - | <StructureSection load='1e66' size='340' side='right' caption='[[1e66]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='1e66' size='340' side='right'caption='[[1e66]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1e66]] 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=1E66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E66 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1e66]] 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=1E66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E66 FirstGlance]. <br> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ace|3ace]], [[2dfp|2dfp]], [[2ace|2ace]], [[2ack|2ack]], [[1vxo|1vxo]], [[1vxr|1vxr]], [[1vot|1vot]], [[1som|1som]], [[1qti|1qti]], [[1qig|1qig]], [[1qih|1qih]], [[1qii|1qii]], [[1qij|1qij]], [[1qik|1qik]], [[1qim|1qim]], [[1qid|1qid]], [[1qie|1qie]], [[1qif|1qif]], [[1oce|1oce]], [[1fss|1fss]], [[1eve|1eve]], [[1eea|1eea]], [[1dx6|1dx6]], [[1cfj|1cfj]], [[1ax9|1ax9]], [[1amn|1amn]], [[1e3q|1e3q]], [[4ace|4ace]], [[1acj|1acj]], [[1acl|1acl]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ace|3ace]], [[2dfp|2dfp]], [[2ace|2ace]], [[2ack|2ack]], [[1vxo|1vxo]], [[1vxr|1vxr]], [[1vot|1vot]], [[1som|1som]], [[1qti|1qti]], [[1qig|1qig]], [[1qih|1qih]], [[1qii|1qii]], [[1qij|1qij]], [[1qik|1qik]], [[1qim|1qim]], [[1qid|1qid]], [[1qie|1qie]], [[1qif|1qif]], [[1oce|1oce]], [[1fss|1fss]], [[1eve|1eve]], [[1eea|1eea]], [[1dx6|1dx6]], [[1cfj|1cfj]], [[1ax9|1ax9]], [[1amn|1amn]], [[1e3q|1e3q]], [[4ace|4ace]], [[1acj|1acj]], [[1acl|1acl]]</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e66 OCA], [http://pdbe.org/1e66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e66 RCSB], [http://www.ebi.ac.uk/pdbsum/1e66 PDBsum]</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=1e66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e66 OCA], [http://pdbe.org/1e66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e66 RCSB], [http://www.ebi.ac.uk/pdbsum/1e66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e66 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/1e66_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e6/1e66_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/ | + | </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=1e66 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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==See Also== | ==See Also== | ||
*[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | *[[AChE inhibitors and substrates|AChE inhibitors and substrates]] | ||
| - | *[[Acetylcholinesterase|Acetylcholinesterase]] | + | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
[[Category: Dvir, H]] | [[Category: Dvir, H]] | ||
Revision as of 07:16, 3 April 2019
STRUCTURE OF ACETYLCHOLINESTERASE COMPLEXED WITH (-)-HUPRINE X AT 2.1A RESOLUTION
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