Now, as we discussed previously, it's the presence of of the catalytic triad inside the active side of Chimetrypsin that actually gives it the power of catalysis, gives it the ability to actually cleave those peptide bonds. So remember, the catalytic triad is basically this collection of three individual residues aspartate HistoGene and Serene, which work together to basically promote the cleavage of those peptide bonds. Now, the question still remains what exactly gives Chimotrypsin its specificity? What gives Chimotrypsin the ability to only Cleave on the carboxyl end of specific amino acids, those amino acids that contain bulky hydrophobic side chain groups? Now, to answer this question, we actually have to study the shape of the active side, the structure of that enzyme. If we examine the active side of that enzyme, we're going to find something called the S one pocket.