3IJ8

Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase

Summary for 3IJ8

Entry DOI	10.2210/pdb3ij8/pdb
Related	3IJ7 3IJ9
Descriptor	Pancreatic alpha-amylase, (2R,3S,4R,5R,6R)-2,6-difluoro-2-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol, 5-fluoro-alpha-L-idopyranose, ... (6 entities in total)
Functional Keywords	amylase, covalent intermediate, hydrolytic cleavage, catalysis, inhibitor synthesis, enzyme kinetics, human digestion, diabetes, obesity, calcium, carbohydrate metabolism, chloride, disulfide bond, glycoprotein, glycosidase, hydrolase, metal-binding, pyrrolidone carboxylic acid, secreted
Biological source	Homo sapiens (human)
Total number of polymer chains	1
Total formula weight	56805.39
Authors	Li, C.,Zhang, R.,Withers, S.G.,Brayer, G.D. (deposition date: 2009-08-04, release date: 2009-10-27, Last modification date: 2020-07-29)
Primary citation	Zhang, R.,Li, C.,Williams, L.K.,Rempel, B.P.,Brayer, G.D.,Withers, S.G. Directed "in situ" inhibitor elongation as a strategy to structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic alpha-amylase Biochemistry, 48:10752-10764, 2009 Cited by PubMed: 19803533 DOI: 10.1021/bi901400p PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.43 Å)

Structure validation