4ara | pdb_00004ara

Mus musculus Acetylcholinesterase in complex with (R)-C5685 at 2.5 A resolution.

spinqualitylabelsall models 4ara, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ara is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, C56, CL, EDO, NAG, PEG Related: 1c2b, 1c2o, 1j06, 1j07, 1ku6, 1maa, 1mah, 1n5m, 1n5r, 1q83, 1q84, 2c0p, 2c0q, 2h9y, 2ha0, 2ha2, 2ha3, 2ha4, 2ha5, 2ha6, 2ha7, 2jey, 2jez, 2jf0, 2jge, 2jgf, 2jgg, 2jgh, 2jgi, 2jgj, 2jgk, 2jgl, 2jgm, 2whp, 2whq, 2whr, 2wls, 2wu3, 2wu4, 2xud, 2xuf, 2xug, 2xuh, 2xui, 2xuj, 2xuk, 2xuo, 2xup, 2xuq, 4a16, 4a23, 4arb Activity: Acetylcholinesterase, with EC number 3.1.1.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ACES_MOUSE] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Publication Abstract from PubMed Take a closer look: Unexpectedly, a pair of enantiomeric ligands proved to have similar binding affinities for acetylcholinesterase. Further studies indicated that the enantiomers exhibit different thermodynamic profiles. Analyses of the noncovalent interactions in the protein-ligand complexes revealed that these differences are partly due to nonclassical hydrogen bonds between the ligands and aromatic side chains of the protein. Similar but Different: Thermodynamic and Structural Characterization of a Pair of Enantiomers Binding to Acetylcholinesterase.,Berg L, Niemiec MS, Qian W, Andersson CD, Wittung-Stafshede P, Ekstrom F, Linusson A Angew Chem Int Ed Engl. 2012 Nov 19. doi: 10.1002/anie.201205113. PMID:23161758 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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