You are trying to dock two proteins which are modelled. Statistically, the reliability of the result already dropped to 50%. Let me explain in details. In a high resolution X-ray crystal structure one may obtain 100% reliability regarding the positions of the atoms. But a homology model gives a maximum score of around 0.8 (80%). Therefore, the possibility of both the modeled structure being true becomes 0.8*0.8 = 0.64 (assuming that you have managed to obtained the best homology models). Now, even if you manage to obtain the best possible docked structure with a very high reliability of say 80%, the overall reliability of the docked complex becomes 0.64*0.8=0.51.
Visualization of the binding geometries and interactions are mandatory. The binding site analysis is also important. Protein-protein interaction plots might show one of the reliable ways to analyze docking results.
You are trying to dock two proteins which are modelled. Statistically, the reliability of the result already dropped to 50%. Let me explain in details. In a high resolution X-ray crystal structure one may obtain 100% reliability regarding the positions of the atoms. But a homology model gives a maximum score of around 0.8 (80%). Therefore, the possibility of both the modeled structure being true becomes 0.8*0.8 = 0.64 (assuming that you have managed to obtained the best homology models). Now, even if you manage to obtain the best possible docked structure with a very high reliability of say 80%, the overall reliability of the docked complex becomes 0.64*0.8=0.51.