Since the evaluation of ligand conformations is a crucial aspect of structure-based virtual screening, scoring functions play significant roles in it. However, it is known that a scoring function does not always work well for all target proteins. When one cannot know which scoring function works best against a target protein a priori, there is no standard scoring method to know it even if 3D structure of a target protein-ligand complex is available. Therefore, development of the method to achieve high enrichments from given scoring functions and 3D structure of protein-ligand complex is a crucial and challenging task. To address this problem, we applied SCS (supervised consensus scoring), which employs a rough linear correlation between the binding free energy and the root-mean-square deviation (rmsd) of a native ligand conformations and incorporates protein-ligand binding process with docked ligand conformations using supervised learning, to virtual screening. We evaluated both the docking poses and enrichments of SCS and five scoring functions (F-Score, G-Score, D-Score, ChemScore, and PMF) for three different target proteins: thymidine kinase (TK), thrombin (thrombin), and peroxisome proliferator-activated receptor gamma (PPARgamma). Our enrichment studies show that SCS is competitive or superior to a best single scoring function at the top ranks of screened database. We found that the enrichments of SCS could be limited by a best scoring function, because SCS is obtained on the basis of the five individual scoring functions. Therefore, it is concluded that SCS works very successfully from our results. Moreover, from docking pose analysis, we revealed the connection between enrichment and average centroid distance of top-scored docking poses. Since SCS requires only one 3D structure of protein-ligand complex, SCS will be useful for identifying new ligands.