1FSS

ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH FASCICULIN-II

Summary for 1FSS

• Entry DOI: 10.2210/pdb1fss/pdb
• Descriptor: ACETYLCHOLINESTERASE, FASCICULIN II, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: complex (serine esterase-toxin), complex (serine esterase-toxin) complex, complex (serine esterase/toxin)
• Biological source: Torpedo californica (Pacific electric ray); More
• Cellular location: Isoform H: Cell membrane; Lipid-anchor, GPI- anchor. Isoform T: Cell membrane; Peripheral membrane protein: P04058
• Total number of polymer chains: 2
• Total formula weight: 67857.31

Authors

Harel, M.,Kleywegt, G.J.,Silman, I.,Sussman, J.L. (deposition date: 1995-10-25, release date: 1996-03-08, Last modification date: 2024-10-23)

Primary citation

Harel, M.,Kleywegt, G.J.,Ravelli, R.B.,Silman, I.,Sussman, J.L.
Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target.
Structure, 3:1355-1366, 1995

PubMed Abstract: Fasciculin (FAS), a 61-residue polypeptide purified from mamba venom, is a three-fingered toxin which is a powerful reversible inhibitor of acetylcholinesterase (AChE). Solution of the three-dimensional structure of the AChE/FAS complex would provide the first structure of a three-fingered toxin complexed with its target.

PubMed: 8747462
DOI: 10.1016/S0969-2126(01)00273-8

Experimental method

X-RAY DIFFRACTION (3 Å)