Talk:Structural Biochemistry/Enzyme/Catalytic Triad and S1 Pocket

Are you kidding me? Why are there no amino acid residues within chymotrypsin s1 binding pocket? It means any peptide possible can interact with S1 pocket and eventually can be cleaved. As far as I know, S1' and S2 binding pockets are also not that selective in contrast to other proteases. Pro in S1' can be sometimes challenging, but no other amino acids. Then, how do you think chymotrypsin is specific for Phe, Trp and Tyr?