4ara

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 Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: 1PE, C56, CL, EDO, NAG, PEG 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. See Also Acetylcholinesterase 3D structures

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