Understanding the Energetic Components Influencing the Thermodynamic Quantities of Carbonic Anhydrase Protein upon Ligand Binding.

We perform structural analysis and calculate the vibrational energy diffusivities, represented as heat‐communication map, between a carbonic anhydrase II and its binding inhibitor benzosulfonamide, to identify critical residues involved in the secondary and tertiary adaptations surrounding the active site, such as HID95, HIE118, HID93, THR197, and HIE198. Notably, the water molecules surrounding the active sites play an essential part in the energy flow. The stability of the docked ligand is assessed using its structural deviation and free energy calculation. Additionally, density functional theory calculations are used to evaluate specific binding energies, resulting in prominent residues such as THR197, THR198, and HIE118 with high binding potential to the benzosulfonamide ligand. [ABSTRACT FROM AUTHOR]