The amylase molecule shown in 3-D using Jmol

The human pancreatic amylase molecule consists of 496 amino acid residues. Click below for different display options

Protein display options
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Primary structure
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Secondary structure
Cartoon format - a helices red, ß sheets gold
Note especially the central barrel-shaped section through which the substrate presumably passes as it is fed into the active site.
Tertiary structure
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Active site
Rotate molecule to look down into active site
The following amino acid residues have been identified (reference below) as contributing to the conversion of glucose polysaccharides (amylose, starch) into disacccharides (maltose). Interestingly, they all have acidic side-chains (aspartic acid and glutamic acid).
Show / hide ASP 197, GLU 233 & ASP300 at active site (white spacefill)
Show / hide enzyme co-factors: calcium (orange) and chloride (turquoise) ions
Show / hide glucose dimer (maltose - the product of starch hydrolysis) red and grey


Reference: Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques. Brayer GD, Sidhu G, Maurus R, Rydberg EH, Braun C, Wang Y, Nguyen NT, Overall CM, Withers SG.

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