Fig. 14 | Scientific Reports

Fig. 14

From: Integrating computational approaches to uncover β-lactamase-associated resistance in diarrheagenic Escherichia coli from pediatric patients

Fig. 14

Docking interactions of ceftriaxone with the AmpC β-lactamase protein. (A) 2D Interactions: Depicts the molecular interactions between ceftriaxone and active site residues of AmpC, including hydrogen bonds, van der Waals forces, π-alkyl interactions, and other stabilizing forces. These interactions play a key role in forming the drug-enzyme complex. Generated using Discovery Studio Visualizer. (B) 3D Interactions: Highlights the spatial orientation of ceftriaxone within the AmpC active site, showing its proximity to key residues involved in stabilizing the binding interaction. Visualized using PyMOL. (C) Surface Area Interactions: Shows the binding pocket topology of AmpC, emphasizing hydrophilic and hydrophobic regions that interact with ceftriaxone. Generated using AutoDock Tools and visualized with PyMOL. (D) Protein Structure with Binding Site: Provides an overview of the AmpC β-lactamase protein, pinpointing the binding pocket and illustrating the interactions of ceftriaxone with surrounding residues in the tertiary structure. Visualized using PyMOL.

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