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3m3d
From Proteopedia
(Difference between revisions)
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<StructureSection load='3m3d' size='340' side='right'caption='[[3m3d]], [[Resolution|resolution]] 2.34Å' scene=''> | <StructureSection load='3m3d' size='340' side='right'caption='[[3m3d]], [[Resolution|resolution]] 2.34Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3m3d]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3m3d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M3D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M3D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> | + | </td></tr><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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3m3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m3d OCA], [https://pdbe.org/3m3d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m3d RCSB], [https://www.ebi.ac.uk/pdbsum/3m3d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m3d ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/ACES_TORCA ACES_TORCA]] 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. |
==See Also== | ==See Also== | ||
Revision as of 13:43, 4 May 2022
Crystal structure of Acetylcholinesterase in complex with Xenon
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Categories: Acetylcholinesterase | Large Structures | Torpedo californica | Behnen, J | Brumshtein, B | Heine, A | Klebe, G | Silman, I | Sussman, J L | Toker, L | Alpha/beta hydrolase | Cell junction | Cell membrane | Disulfide bond | Glycoprotein | Glycosylated protein | Gpi-anchor | Hydrolase | Lipoprotein | Membrane | Neurotransmitter degradation | Protein-xe complex | Serine esterase | Synapse
