3IJ7

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

Summary for 3IJ7

• Entry DOI: 10.2210/pdb3ij7/pdb
• Related: 3IJ8 3IJ9
• Descriptor: Pancreatic alpha-amylase, 4-O-methyl-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-2)-5-fluoro-alpha-L-idopyranose, 4-O-methyl-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranosyl fluoride, ... (6 entities in total)
• Functional Keywords: amylase, covalent intermediate, hydrolytic cleavage, catalysis, inhibitor synthesis, enzyme kinetics, human digestion, diabetes, obesity, 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: 56901.60

Authors

Li, C.,Zhang, R.,Withers, S.G.,Brayer, G.D. (deposition date: 2009-08-03, 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; PubMed: 19803533; DOI: 10.1021/bi901400p

Experimental method

X-RAY DIFFRACTION (2 Å)