4ara
From Proteopedia
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| - | [[Image:4ara.jpg|left|200px]] | ||
| - | + | ==Mus musculus Acetylcholinesterase in complex with (R)-C5685 at 2.5 A resolution.== | |
| + | <StructureSection load='4ara' size='340' side='right'caption='[[4ara]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ara]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ARA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARA FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=C56:4-(DIMETHYLAMINO)-N-{[(2R)-1-ETHYLPYRROLIDIN-2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE'>C56</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></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=4ara FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ara OCA], [https://pdbe.org/4ara PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ara RCSB], [https://www.ebi.ac.uk/pdbsum/4ara PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ara ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Take a closer look: Unexpectedly, a pair of enantiomeric ligands proved to have similar binding affinities for acetylcholinesterase. Further studies indicated that the enantiomers exhibit different thermodynamic profiles. Analyses of the noncovalent interactions in the protein-ligand complexes revealed that these differences are partly due to nonclassical hydrogen bonds between the ligands and aromatic side chains of the protein. | ||
| - | + | Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase.,Berg L, Niemiec MS, Qian W, Andersson CD, Wittung-Stafshede P, Ekstrom F, Linusson A Angew Chem Int Ed Engl. 2012 Nov 19. doi: 10.1002/anie.201205113. PMID:23161758<ref>PMID:23161758</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4ara" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Andersson | + | [[Category: Andersson CD]] |
| - | [[Category: Berg | + | [[Category: Berg L]] |
| - | [[Category: Ekstrom | + | [[Category: Ekstrom F]] |
| - | [[Category: Linusson | + | [[Category: Linusson A]] |
| - | [[Category: Niemiec | + | [[Category: Niemiec MS]] |
| - | [[Category: Qian | + | [[Category: Qian W]] |
| - | [[Category: | + | [[Category: WittungStafshede P]] |
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Current revision
Mus musculus Acetylcholinesterase in complex with (R)-C5685 at 2.5 A resolution.
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