Draw the hydrogen bonds. The structure probably contains an inhibitor bound in the catalytic site because a protease has to be inhibited during the crystallization or it will self-hydrolyze. Include the inhibitor in the figure. Measure interaction distances between the residues of the catalytic triad and between the protein and the inhibitor, or any solvent molecules contained within the active site. Indicate which interactions are hydrogen bonds.
Many serine proteases are self-digesting.
However, chymotrypsin exhibits less self-digestion than trypsin and elastase, for example. Provide an explanation for this phenomenon. Define the specific reaction that is catalyzed by the serine protease that you selected. Propose the structure of a potential inhibitor for the serine protease that you selected. Explain why this proposed structure might make a good inhibitor for the enzyme.