So this is not functional because its active side does not have the correct orientation. And the oxyanion hole that is used to basically stabilize the tetrahedral intermediate is not formed. And so what must happen is to actually activate the enzyme activity of this molecule, trypsin and active form another digestive enzyme basically must cleave at a single peptide bond this inactive chymatrypcinogen. And so what it does is it cleaves the peptide bond between the 15th and the 16th amino acid. Now, the 15th amino acid is arginine and the 16th amino acid is isolucine. So the bond holding these two amino acids is cleaved by Trypsin and this activates this Zymogen to form something we call pychiamitrypsin.