1ua3 | pdb_00001ua3

Crystal structure of the pig pancreatic a-amylase complexed with malto-oligosaccharides

spinqualitylabelsall models 1ua3, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ua3 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.01Å Ligands: BGC, CA, CL, EDO, GLC, PRD_900001, PRD_900009 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMYP_PIG 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 The structural X-ray map of a pig pancreatic alpha-amylase crystal soaked (and flash-frozen) with a maltopentaose substrate showed a pattern of electron density corresponding to the binding of oligosaccharides at the active site and at three surface binding sites. The electron density region observed at the active site, filling subsites-3 through-1, was interpreted in terms of the process of enzyme-catalyzed hydrolysis undergone by maltopentaose. Because the expected conformational changes in the "flexible loop" that constitutes the surface edge of the active site were not observed, the movement of the loop may depend on aglycone site being filled. The crystal structure was refined at 2.01 A resolution to an R factor of 17.0% ( R(free) factor of 19.8%). The final model consists of 3910 protein atoms, one calcium ion, two chloride ions, 103 oligosaccharide atoms, 761 atoms of water molecules, and 23 ethylene glycol atoms. Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaccharides.,Payan F, Qian M J Protein Chem. 2003 Apr;22(3):275-84. PMID:12962327 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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