The 3-dimensional structure of the amylase molecule

The human pancreatic amylase molecule consists of 496 amino acid residues.
This molecule can be moved by holding down the left mouse button and dragging. The right button gives many options.
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Protein display options
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Primary structure
Colour each amino acid .... Show residue numbers .... Show residue names ... Remove labels & restore default colours
Secondary structure
Cartoon format coloured by structure - α helices pinkish red, other helices purple/dark blue, β 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
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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

Web references

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.


Possibly relevant
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(from Amazon.co.uk)