1W75
Native Orthorhombic form of Torpedo californica acetylcholinesterase (AChE)
Summary for 1W75
| Entry DOI | 10.2210/pdb1w75/pdb |
| Related | 1ACJ 1ACL 1AMN 1AX9 1CFJ 1DX6 1E3Q 1E66 1EA5 1EEA 1EVE 1FSS 1GPK 1GPN 1GQR 1GQS 1H22 1H23 1HBJ 1JGA 1JGB 1JJB 1OCE 1ODC 1QID 1QIE 1QIF 1QIG 1QIH 1QII 1QIJ 1QIK 1QIM 1QTI 1SOM 1UT6 1VOT 1VXO 1VXR 1W4L 1W6R 1W76 2ACE 2ACK 2DFP 3ACE 4ACE |
| Descriptor | ACETYLCHOLINESTERASE, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | alzheimer's disease, cholinesterase, glycoprotein, gpi- anchor, hydrolase, muscle, nerve, neurotransmitter degradation, serine esterase, serine hydrolase, synapse |
| Biological source | TORPEDO CALIFORNICA (PACIFIC ELECTRIC RAY) |
| Total number of polymer chains | 2 |
| Total formula weight | 123535.01 |
| Authors | Greenblatt, H.M.,Botti, S.,Argaman, A.,Silman, I.,Sussman, J.L. (deposition date: 2004-08-29, release date: 2004-11-25, Last modification date: 2024-11-20) |
| Primary citation | Greenblatt, H.M.,Guillou, C.,Guenard, D.,Argaman, A.,Botti, S.,Badet, B.,Thal, C.,Silman, I.,Sussman, J.L. The complex of a bivalent derivative of galanthamine with torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design. J.Am.Chem.Soc., 126:15405-15411, 2004 Cited by PubMed Abstract: Bifunctional derivatives of the alkaloid galanthamine, designed to interact with both the active site of the enzyme acetylcholinesterase (AChE) and its peripheral cation binding site, have been assayed with Torpedo californica AChE (TcAChE), and the three-dimensional structures of their complexes with the enzyme have been solved by X-ray crystallography. Differences were noted between the IC(50) values obtained for TcAChE and those for Electrophorus electricus AChE. These differences are ascribed to sequence differences in one or two residues lining the active-site gorge of the enzyme. The binding of one of the inhibitors disrupts the native conformation of one wall of the gorge, formed by the loop Trp279-Phe290. It is proposed that flexibility of this loop may permit the binding of inhibitors such as galanthamine, which are too bulky to penetrate the narrow neck of the gorge formed by Tyr121 and Phe330 as seen in the crystal structure. PubMed: 15563167DOI: 10.1021/ja0466154 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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