Fig. 3.

Molecular docking and dynamics simulation of ginkgetin binding to STEAP2 (A) Predicted binding conformation of ginkgetin within the STEAP2 protein, highlighting key interacting amino acid residues. B Root mean square deviation (RMSD) of the STEAP2–ginkgetin complex during the 100-ns molecular dynamics simulation. C Radius of gyration (Rg) of the STEAP2–ginkgetin complex over the simulation time, reflecting structural compactness. D Solvent-accessible surface area (SASA) changes of the complex during the simulation. E Root mean square fluctuation (RMSF) of individual STEAP2 residues, indicating local flexibility. F Number of hydrogen bonds formed between ginkgetin and STEAP2 throughout the simulation