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3i6m
From Proteopedia
(Difference between revisions)
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==3D Structure of Torpedo californica acetylcholinesterase complexed with N-piperidinopropyl-galanthamine== | ==3D Structure of Torpedo californica acetylcholinesterase complexed with N-piperidinopropyl-galanthamine== | ||
<StructureSection load='3i6m' size='340' side='right' caption='[[3i6m]], [[Resolution|resolution]] 2.26Å' scene=''> | <StructureSection load='3i6m' size='340' side='right' caption='[[3i6m]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w4l|1w4l]], [[1w6r|1w6r]], [[1qti|1qti]], [[1w76|1w76]], [[1dx6|1dx6]], [[3i6z|3i6z]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w4l|1w4l]], [[1w6r|1w6r]], [[1qti|1qti]], [[1w76|1w76]], [[1dx6|1dx6]], [[3i6z|3i6z]]</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=3i6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i6m RCSB], [http://www.ebi.ac.uk/pdbsum/3i6m 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=3i6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i6m OCA], [http://pdbe.org/3i6m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i6m RCSB], [http://www.ebi.ac.uk/pdbsum/3i6m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i6m ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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<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=3i6m 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3i6m" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Acetylcholinesterase|Acetylcholinesterase]] | *[[Acetylcholinesterase|Acetylcholinesterase]] | ||
| + | *[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:41, 5 August 2016
3D Structure of Torpedo californica acetylcholinesterase complexed with N-piperidinopropyl-galanthamine
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Categories: Acetylcholinesterase | Torpedo californica | Bartolucci, C | Lamba, D | Alzheimer's disease | Bis-functional galanthamine derivative | Cell junction | Cell membrane | Cholinesterase | Disulfide bond | Glycoprotein | Gpi-anchor | Hydrolase | Lipoprotein | Membrane | Neurotransmitter degradation | Serine esterase | Serine hydrolase | Synapse
