## 3 Results and Discussion
### Molecular Docking Studies  
The analysis of the docking results revealed that among all seven targets, only thymidyllate kinase (TMK) from _P. aeruginosa_ showed good binding affinity and docking interactions with studied complexes. The results of the docking scores of control inhibitor and silver complexes against the target proteins are mentioned in the Table 3. Figure 12D presents the alignment of different silver complexes in the active site of TMK. As shown in the Figure 12A-C, all the complexes fit well into the active site of TMK. The coordinates of these compounds overlap in the crystal structure of the template plate, mimicking some of its interactions with the macromolecule. \begin{table}
\begin{tabular}{c c c c c c} \hline  & & & & \multicolumn{3}{c}{**Docking Scores**} \\ \cline{2-6}
**PDB ID Codes** & \multicolumn{2}{c}{**RMSD of Control Ligand**} & \multicolumn{3}{c}{**Silver (I) Complexes**} \\ \cline{2-6}  & **(Å)** & **Control Ligand** & **1** & **2** & **3** \\ \hline
1 TYL & 1.85 & \(-\)11.6752 & \(-\)7.224 & \(-\)10.1026 & \(-\)7.7626 \\
1 BNA & - & - & \(-\)5.7922 & \(-\)7.2206 & \(-\)4.3620 \\
3 FYV & 1.23 & \(-\)8.4286 & \(-\)6.8618 & \(-\)9.6077 & \(-\)5.3467 \\
3 UWK & 0.9 & \(-\)10.9856 & \(-\)8.1865 & \(-\)11.4224 & \(-\)6.2362 \\
4 HOF & 1.5 & \(-\)8.6736 & \(-\)5.9142 & \(-\)7.8969 & \(-\)4.9028 \\
4 URM & 1.9 & \(-\)9.4327 & \(-\)6.7318 & \(-\)8.0604 & \(-\)4.881 \\
4H2M & 2.0 & \(-\)10.6792 & \(-\)5.7233 & \(-\)9.2959 & \(-\)4.8587 \\ \hline \end{tabular}
\end{table} 
Table 3: Root-mean-square deviation (RMSD) and predicted binding affinity (docking scores in kcal/mol) of control inhibitor and silver complexes against target proteins. Figure 11: Overview of the antibacterial test showing Minimum Inhibitory Concentrations (MIC) in \(\mu\)g/mL, thus lowest values corresponding to the most active compounds. The binding mode of complex **1** with thymidyllate kinase displayed number of prominent interactions including hydrophobic, hydrophilic, salt bridges, and \(\pi\)- stacking interactions. Figure 12A presented that O\({}_{3}\) of the nitrate anion that directly ligated to the silver metal involved in hydrogen bond interaction with the side chain of Arg50 (2.73 and 2.95 A), Arg96 (3.23 A), and Arg151 (2.85 A), respectively. While Tyr104 mediate strong hydrogen bond interaction with the carbonyl of pyridine-3-carboxaldehyde at a distance of 2.07 A. The hydrophobic contact of pyridine ring with Glu12, Arg96, Phe155, and Glu156 might also contribute in the observed activity of this complex. Further protein-ligand interactions are stabilized by the formation of a salt bridge between complex and Glu12 and Asp153. Moreover, the geometry of the silver metal interaction retained by making contact with Asp153 at a distance of 2.78 A. In case of most active complex **2**, a network of strong hydrogen bond interactions with the residues of the active site of TMK has been observed that rationalize the inhibitory potential of the complex. The nitrate ion of the complex involved in three hydrogen bond interactions with Tyr104, side chain of Glu12, and Arg96 at a distance of 1.88, 2.19, and 2.46 A, respectively. Both of the nitrate ions that ligated with silver metal mediated bidentate hydrogen bond interactions with the residues Glu12 (3.02 A), Arg50 (2.99 A), Arg96 (2.66 A), Arg149 (2.80 and 2.88 A), and Glu156 (3.41 A). The hydrophobic contact of pyridone rings with the hydrophobic patch of Pro11, Ala100, Tyr104, Ala146, Arg151, Phe155, and Phe163 provided further anchorage to the active site. Complex **2** was further stabilized by special type of electrostatic interactions i.e., salt bridges between pyridone of the complex with Glu12, Asp153, and Glu156 (Figure 12B). Figure 12: Binding patterns of (**A**) Complex **1**, (**B**) Complex **2**, and (**C**) Complex **3** with thymidyllate kinase (TMK) of _P. aeruginosa_ demonstrated from the top ranked dock pose. Red dashed lines represent H-bonds, while (**D**) presents the superimposition of all the compounds.