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5hcu
From Proteopedia
(Difference between revisions)
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<StructureSection load='5hcu' size='340' side='right'caption='[[5hcu]], [[Resolution|resolution]] 2.42Å' scene=''> | <StructureSection load='5hcu' size='340' side='right'caption='[[5hcu]], [[Resolution|resolution]] 2.42Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5hcu]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5hcu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5dtg 5dtg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HCU FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4151Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MIS:MONOISOPROPYLPHOSPHORYLSERINE'>MIS</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hcu OCA], [https://pdbe.org/5hcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hcu RCSB], [https://www.ebi.ac.uk/pdbsum/5hcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hcu 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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Acetylcholinesterase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Tong | + | [[Category: Tong L]] |
| - | [[Category: Tran | + | [[Category: Tran TH]] |
| - | + | ||
Current revision
Crystal structure of mouse acetylchoinesterase inhibited by DFP
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