Fig. 23.2 The surface of the trypsin-like serine proteases trypsin, thrombin, factor VIIa, and factor Xa display deep po...
Fig. 23.5 Crystal structure of the inhibitor cyclotheonamide A with thrombin. The inhibitor forms a covalent bond to the...
Fig. 23.6 General binding mode of a peptide chain that is to be cleaved (gray carbon atoms) in the catalytic site of a s...
Fig. 23.7 Comparison of the binding mode of the irreversibly binding thrombin inhibitors D-Phe–Pro–Arg-CH2Cl (dark-r...
Fig. 23.10 Structure of the thrombin–NAPAP complex. The most important interactions are outlined on the left side. The...
Fig. 23.12 Comparison of the 3D structures of trypsin (left) and thrombin (right), each in complex with NAPAP. The activ...
Fig. 23.17 The crystal structure of 23.27 (Fig. 23.16) in complex with elastase. The inhibitor forms two H-bonds to Val2...
Fig. 23.19 Crystal structure of rivaroxaban 23.30 (Fig. 23.19) in factor Xa. The inhibitor’s chlorothiophene group bin...
Fig. 23.23 In the last step of the bacterial cell wall synthesis, a glycopeptide transpeptidase cleaves the bond between...
Fig. 23.24 Unsubstituted penicillic acid 23.48 is quickly cleaved by TEM-1β-lactamase (a). By adding a hydroxymethyl g...
Fig. 23.26 The proteasome, a cellular shredding machine, proteolytically cleaves ubiquitinylated proteins selectively in...
Fig. 23.28 Crystallographically determined binding mode of nirmatrelvir 23.61 to the SARS-Cov-2 Mpro major protease. The...