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Structure paper

TitleDirected "in situ" inhibitor elongation as a strategy to structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic alpha-amylase
Journal, issue, pagesBiochemistry, Vol. 48, Page 10752-10764, Year 2009
Publish dateAug 3, 2009 (structure data deposition date)
AuthorsZhang, R. / Li, C. / Williams, L.K. / Rempel, B.P. / Brayer, G.D. / Withers, S.G.
External linksBiochemistry / PubMed:19803533
MethodsX-ray diffraction
Resolution1.43 - 2 Å
Structure data

PDB-3ij7:
Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3ij8:
Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
Method: X-RAY DIFFRACTION / Resolution: 1.43 Å

PDB-3ij9:
Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-B0D:
(2R,3S,4R,5R,6R)-2,6-difluoro-2-(hydroxymethyl)tetrahydro-2H-pyran-3,4,5-triol

ChemComp-B9D:
5-fluoro-alpha-L-idopyranose

Source
  • homo sapiens (human)
KeywordsHYDROLASE / amylase / covalent intermediate / hydrolytic cleavage / catalysis / inhibitor synthesis / enzyme kinetics / human digestion / diabetes / obesity / Carbohydrate metabolism / Chloride / Disulfide bond / Glycoprotein / Glycosidase / Metal-binding / Pyrrolidone carboxylic acid / Secreted / Calcium

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