A specific stereochemical arrangement of amino acid residues in serine proteases that is characterisic of this class of proteases and that is responsible for their catalytic activity.
The residues are:
- The hydroxyl group of the serine side chain serves as the nucleophile that attacks the relatively electron-deficient carbonyl carbon of the peptide bond.
- The histidine side chain is juxtaposed to the serine hydroxyl in such a way as to enhance its nucleophilicity.
- aspartic acid.
- The aspartate side chain is close to the imidazole group assisting its ability to act as a proton acceptor.