Fig. 23.10
From: Inhibitors of Hydrolases with an Acyl–Enzyme Intermediate
Structure of the thrombin–NAPAP complex. The most important interactions are outlined on the left side. The positively charged benzamidine group occupies the S1 pocket and forms a salt bridge to the negatively charged side chain of Asp189. Two hydrogen bonds are formed to the amino acid Gly216. The piperidyl and naphthyl groups together occupy the two large lipophilic pockets S2 and S3.