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![[Figure 4]](ud5045fig4mag.jpg)
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Figure 4
(a) Sequence and chemical structure of the MAM-117 inhibitor. The P1 residue that contains the α-ketoamide moiety is in red. Ac and all correspond to acetyl and allyl, respectively. (b) Crystal structure of PvS1Cat-Tryps (depicted as a green surface) in complex with the inhibitor MAM-117 (yellow). (c) Electron density of chain A of the receptor (PvS1Cat-Tryps catalytic groove) coupled to its ligand (MAM-117 inhibitor) within the asymmetric unit of PvS1Cat-Tryps–MAM-117. (d) PvS1Cat-Tryps residues (in green) involved in the interaction with MAM-117 (in yellow). Hydrogen bonds are depicted as blue dotted lines. The P4–P2′ positions of MAM-117 are indicated. (e) LigPlot+ analysis of the interactions of the MAM-117 inhibitor (blue lines) with the catalytic active site of PvS1Cat-Tryps (green residues) (Laskowski & Swindells, 2011  ). The covalent bond between the catalytic Ser549 residue of PvS1Cat-Tryps and the α-ketoamide moiety of MAM-117 is shown as a purple line. Hydrogen bonds are depicted as green dotted lines and hydrophobic interactions as red semicircles. The P4 to P2′ positions of MAM-117 are shown in grey or light blue. |
![[Figure 4]](ud5045fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
