4EY8
Crystal structure of recombinant human acetylcholinesterase in complex with fasciculin-2
Summary for 4EY8
| Entry DOI | 10.2210/pdb4ey8/pdb |
| Descriptor | Acetylcholinesterase, Fasciculin-2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | acetylcholinesterase, hydrolase, fasciculin 2, snake venom toxin, inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 67554.02 |
| Authors | Cheung, J.,Rudolph, M.,Burshteyn, F.,Cassidy, M.,Gary, E.,Love, J.,Height, J.,Franklin, M. (deposition date: 2012-05-01, release date: 2012-10-17, Last modification date: 2024-11-06) |
| Primary citation | Cheung, J.,Rudolph, M.J.,Burshteyn, F.,Cassidy, M.S.,Gary, E.N.,Love, J.,Franklin, M.C.,Height, J.J. Structures of human acetylcholinesterase in complex with pharmacologically important ligands. J.Med.Chem., 55:10282-10286, 2012 Cited by PubMed Abstract: Human acetylcholinesterase (AChE) is a significant target for therapeutic drugs. Here we present high resolution crystal structures of human AChE, alone and in complexes with drug ligands; donepezil, an Alzheimer's disease drug, binds differently to human AChE than it does to Torpedo AChE. These crystals of human AChE provide a more accurate platform for further drug development than previously available. PubMed: 23035744DOI: 10.1021/jm300871x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5958 Å) |
Structure validation
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