The higher, in absolute value, of delta G, the better the energy of the protein-ligand complex. However, it doesn't correlate with the activity presenting different ligands. A priori, what should correlate, is if you have a ligand A, and the ligand B, the difference in whose delta G (AAG a-b = | dG(a) - dG(b)| ) should correlate better with the activity. No values a priori can be told, as depending of the size of the binding site and the size of your ligand, more contacts, hence, better or worse dG
If the complex protein-ligand is stable, then, molecular dynamics is required. What you need to do is monitorize the RMSD of your ligand, but it won't give so much information.
Essentially, you need to combine dG and RMSD information both together. You could have very good binders that present a good energetic profile (dG) but are less stable (RMSD high) and viceversa. At the end, both descriptors could give you a hint about if the ligand is stable and energetically well stabilized by the protein