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Subtilisin is a protease that initiates the nucleophillic attack on the peptide bond through a serine residue at the active site. It is a 275 residue globular protein with several alpha-helices and a large beta sheet. It's active site is composed of three amino acids, serine, aspartate, and histidine. This is known as a catalytic triad. Which works to break peptide bonds on polypeptides.

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This will show the different secondary structures of the protein. In red the beta sheets are shown and in blue alpha helices are shown. The alpha helices are amphipathic elements.

This shows the hydrophobic interactions of the protein.

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