1AMN

TRANSITION STATE ANALOG: ACETYLCHOLINESTERASE COMPLEXED WITH M-(N,N,N-TRIMETHYLAMMONIO)TRIFLUOROACETOPHENONE

Summary for 1AMN

• Entry DOI: 10.2210/pdb1amn/pdb
• Descriptor: ACETYLCHOLINESTERASE, SULFATE ION, M-(N,N,N-TRIMETHYLAMMONIO)-2,2,2-TRIFLUORO-1,1-DIHYDROXYETHYLBENZENE, ... (4 entities in total)
• Functional Keywords: hydrolase, serine esterase, synapse, membrane, nerve, muscle, neurotransmitter degradation, glycoprotein, gpi-anchor, alternative splicing, hydrolase (serine esterase)
• Biological source: Torpedo californica (Pacific electric ray)
• Cellular location: Isoform H: Cell membrane; Lipid-anchor, GPI- anchor. Isoform T: Cell membrane; Peripheral membrane protein: P04058
• Total number of polymer chains: 1
• Total formula weight: 61082.82

Authors

Harel, M.,Silman, I.,Sussman, J.L. (deposition date: 1996-02-13, release date: 1996-04-03, Last modification date: 2021-06-02)

• Primary citation: Harel, M.,Quinn, D.M.,Nair, H.K.,Silman, I.,Sussman, J.L.; The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase.; J.Am.Chem.Soc., 118:2340-2346, 1996

Experimental method

X-RAY DIFFRACTION (2.8 Å)