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1DHK

STRUCTURE OF PORCINE PANCREATIC ALPHA-AMYLASE

Summary for 1DHK
Entry DOI10.2210/pdb1dhk/pdb
DescriptorPORCINE PANCREATIC ALPHA-AMYLASE, BEAN LECTIN-LIKE INHIBITOR, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
Functional Keywordspancreatic alpha-amylase, porcine, lectin-like inhibitor, complex (hydrolase-inhibitor), complex (hydrolase-inhibitor) complex, complex (hydrolase/inhibitor)
Biological sourceSus scrofa (pig)
More
Total number of polymer chains2
Total formula weight81439.54
Authors
Bompard-Gilles, C.,Payan, F. (deposition date: 1996-10-14, release date: 1997-12-24, Last modification date: 2024-10-23)
Primary citationBompard-Gilles, C.,Rousseau, P.,Rouge, P.,Payan, F.
Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex.
Structure, 4:1441-1452, 1996
Cited by
PubMed Abstract: alpha-Amylases catalyze the hydrolysis of glycosidic linkages in starch and other related polysaccharides. The alpha-amylase inhibitor (alpha-Al) from the bean Phaseolus vulgaris belongs to a family of plant defence proteins and is a potent inhibitor of mammalian alpha-amylases. The structure of pig pancreatic alpha-amylase (PPA) in complex with both a carbohydrate inhibitor (acarbose) and a proteinaceous inhibitor (Tendamistat) is known, but the catalytic mechanism is poorly understood.
PubMed: 8994970
DOI: 10.1016/S0969-2126(96)00151-7
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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