2ace | pdb_00002ace

NATIVE ACETYLCHOLINESTERASE (E.C. 3.1.1.7) FROM TORPEDO CALIFORNICA

spinqualitylabelsall models 2ace, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ace is a 1 chain structure with sequence from Torpedo californica. This structure supersedes the now removed PDB entry 1ace. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACH Activity: Acetylcholinesterase, with EC number 3.1.1.7 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed (-)-Huperzine A (HupA) is found in an extract from a club moss that has been used for centuries in Chinese folk medicine. Its action has been attributed to its ability to strongly inhibit acetylcholinesterase (AChE). The crystal structure of the complex of AChE with optically pure HupA at 2.5 A resolution shows an unexpected orientation for the inhibitor with surprisingly few strong direct interactions with protein residues to explain its high affinity. This structure is compared to the native structure of AChE devoid of any inhibitor as determined to the same resolution. An analysis of the affinities of structural analogues of HupA, correlated with their interactions with the protein, shows the importance of individual hydrophobic interactions between HupA and aromatic residues in the active-site gorge of AChE. Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.,Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL Nat Struct Biol. 1997 Jan;4(1):57-63. PMID:8989325 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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OCA, Joel L. Sussman