A spatially organized group of three catalytic residues. Serine proteases commonly use serine, histidine and aspartate, but similar geometry in different folds can reflect convergent evolution.
The catalytic triad is a well-known structural motif found in the active sites of certain enzymes, particularly serine proteases. It consists of three specific amino acid residues that work together to facilitate the enzyme's catalytic activity. The classic catalytic triad includes: 1. **Serine (Ser or S)** - Often the key nucleophile in the reaction, which participates in the formation of a transient enzyme-substrate complex.
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