Figure 5. In-silico modeling of PA with AMPK.

A. PA docked to AMPK by autodoc4. The model used was the AMPK structure with ligands in the PDB entry 4CFF (DOI: 10.1038/ncomms4017, Nature Communications). α is cyan, β is green, γ is magenta and the ligands are gold. Ab. Docking results for the allosteric regulatory γ site. The ligand docks in a highly positive charged site. The nearest residues to the ligand are: Tyr¹²¹ (magenta), Arg⁷⁰, Thr⁸¹, Met⁸⁵, His¹⁵¹, Arg¹⁵². The carboxylate of PA is buried and interacts with Arg¹⁵². Ac. PA binds to the same regulatory site at which AMP (black) binds. Ad. Docking results for the α (kinase) binding site. The nearest residue are the backbone of Val²⁴ at the carboxyl end, and Met⁹³ at the -OH end. The primary interaction is hydrophobic. Ae. PA interferes with the binding site of staurosporine. B. Clustering data of PA to both α and γ subunits of AMPK.