4EY4

Crystal Structure of Recombinant Human Acetylcholinesterase in the Apo state

Summary for 4EY4

Entry DOI	10.2210/pdb4ey4/pdb
Descriptor	Acetylcholinesterase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (7 entities in total)
Functional Keywords	acetylcholinesterase, hydrolase, apo
Biological source	Homo sapiens (human)
Total number of polymer chains	2
Total formula weight	120937.15
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: 2024-11-27)
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: 23035744 DOI: 10.1021/jm300871x PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.156 Å)

Structure validation