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4arb
From Proteopedia
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==Mus musculus Acetylcholinesterase in complex with (S)-C5685 at 2.25 A resolution.== | ==Mus musculus Acetylcholinesterase in complex with (S)-C5685 at 2.25 A resolution.== | ||
| - | <StructureSection load='4arb' size='340' side='right' caption='[[4arb]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='4arb' size='340' side='right'caption='[[4arb]], [[Resolution|resolution]] 2.25Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4arb]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4arb]] 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=4ARB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ARB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C57:4-(DIMETHYLAMINO)-N-{[(2S)-1-ETHYLPYRROLIDIN-2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE'>C57</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C57:4-(DIMETHYLAMINO)-N-{[(2S)-1-ETHYLPYRROLIDIN-2-YL]METHYL}-2-METHOXY-5-NITROBENZAMIDE'>C57</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</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=4arb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4arb OCA], [https://pdbe.org/4arb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4arb RCSB], [https://www.ebi.ac.uk/pdbsum/4arb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4arb ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4arb" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4arb" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[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: WittungStafshede | + | [[Category: WittungStafshede P]] |
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Current revision
Mus musculus Acetylcholinesterase in complex with (S)-C5685 at 2.25 A resolution.
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