2HA7
Crystal structure of mutant S203A of mouse acetylcholinesterase complexed with butyrylthiocholine
Summary for 2HA7
Entry DOI | 10.2210/pdb2ha7/pdb |
Related | 1J06 2H9Y 2HA0 2HA2 2HA3 2HA4 2HA5 2HA6 |
Descriptor | Acetylcholinesterase, IODIDE ION, 2-(TRIMETHYLAMMONIUM)ETHYL THIOL, ... (7 entities in total) |
Functional Keywords | hydrolase fold, serine esterase, acetylcholinesterase, mutant, homodimer, glycosylated protein, hydrolase |
Biological source | Mus musculus (house mouse) |
Cellular location | Cell junction, synapse. Isoform H: Cell membrane; Lipid-anchor, GPI- anchor; Extracellular side: P21836 |
Total number of polymer chains | 2 |
Total formula weight | 121718.78 |
Authors | Bourne, Y.,Radic, Z.,Sulzenbacher, G.,Kim, E.,Taylor, P.,Marchot, P. (deposition date: 2006-06-12, release date: 2006-07-18, Last modification date: 2023-10-25) |
Primary citation | Bourne, Y.,Radic, Z.,Sulzenbacher, G.,Kim, E.,Taylor, P.,Marchot, P. Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding J.Biol.Chem., 281:29256-29267, 2006 Cited by PubMed: 16837465DOI: 10.1074/jbc.M603018200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.66 Å) |
Structure validation
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