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 Cited by |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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