Fig. 5: MD simulations of Andro-Rac1.

A RMSD of complex, protein, and Ligand, reflecting structural deviation and conformational stability over time. B Rg of the complex, indicating overall compactness and structural tightness. C Rac1 and Andro binding site distance, monitoring binding stability and positional consistency. D FEL showing a single dominant basin, indicating conformational stability without large-scale reorganization. E Buried area between Andro and Rac1, representing the extent of buried surface and interaction strength. F Simulated conformational superposition, illustrating structural flexibility and binding site variations. G Modeling trajectory change, displaying dynamic shifts in binding site and molecular orientation. H PCA and protein structure, highlighting dominant motion modes and conformational flexibility. I Andro and Rac1 binding energies VDW and ELE, showing contributions from van der Waals and electrostatic interactions. J Hydrogen bond number, reflecting the stability and strength of polar interactions. K Hydrogen bond frequency between Andro and Rac1, indicating persistence and key residues involved in H-bond formation.