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Mechanism of Serine Protease
Description
This template shows the mechanism of serine protease activity within an enzyme's active site, where an aspartate residue hydrogen bonds to histidine, which in turn deprotonates a serine hydroxyl group so it can attack the carbonyl carbon of a peptide substrate bond. Curved red arrows trace the electron movement from the serine oxygen to the substrate carbonyl and from the carbonyl oxygen outward.
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