All of the 20 training set compounds along with the 72 database hits retrieved from the database screening process were docked into the protein active site using the GOLD (Genetic Optimization for Ligand Docking) docking program. GOLD fitness score which differentiates molecules on account of their interacting pattern is calculated for all molecules. The most active compound of training set (compound 1) scored a docking score of 66.6 and exhibited various hydrogen-bonding interactions with the key active site residues (Figure 7a ). Moreover, two of the carbonyl oxygen atoms near the middle ring that mapped on the HBA features of "Hypo1" showed hydrogen-bonding interactions with Gly193 and Ser195 residues of the active site. Previous studies of chymase have also divulged the importance of Gly193 and Ser195 as key amino acids in active site region of the enzyme [9, 13] . Along with diverse hydrogen-bonding contacts, the phenyl group of compound 1, which was mapped on the HY-AR feature of "Hypo1" showed π···σ interactions with the aromatic ring of residue F191. Moreover, compound 1 also showed hydrophobic interactions with Y215 and L99 amino acids. Several hit compounds obtained from database screening process also showed high GOLD fitness scores and formed interactions with the active site residues. The hit compounds that showed a fitness score of more than 66 were selected as final hits for further evaluation process. Intriguingly, all the final three compounds were obtained from Maybridge database and none from the Chembridge database. Compound HTS12673 which showed an estimated activity value of 6.716 nM has scored a GOLD fitness score of 78.73. It has also exhibited key interactions with the important amino acids like Gly193, Ser195, Y215, and H57 at the active site of the enzyme (Figure 7b ). The phenyl part of anisole ring and pyridine ring that mapped over the HY-AR features of "Hypo1" instigated the improved binding of this compound through better hydrophobic interactions. Compound BTB02076, which was also retrieved from the Maybridge database, with an estimated activity value of 8.605 nM has shown a GOLD fitness score of 72.40. This compound has formed various close contacts that lead to the important ligand-enzyme interaction such as hydrogen bonding interactions with Gly193, Ser195 and hydrophobic interactions with Phe191 amino acid in the active site of the enzyme (Figure 7c) . Moreover, important π···π interactions between the fused ring system of BTB02076 and the side chain imidazole ring of His57 amino acid were also revealed. Furthermore, it also showed hydrophobic interactions with Y125 and L99 amino acid residues of protein through the hydrophobic groups mapped over HY-AR features of Hypo1. Third hit, JFD00311, with the estimated activity value of 4.661 nM and GOLD fitness score of 74.51 has formed hydrogen bond network with the active site residues Gly193, and Ser195 (Figure 7d ). The benzene rings and oxygen atoms of the benzenesulfonic acid moieties in this hit compound that overlaid the HY-AR and HBA features of "Hypo1", respectively, enabled considerable hydrophobic and polar interactions with the important amino acids in the active site. The mapping of these top three database final hits on Hypo1 and their 2D molecular structures are depicted in Figures 8 and 9 , respectively. All three hit compounds have mapped the entire features of the best pharmacophore model, Hypo1. Thus, in the design of potent inhibitors of chymase, compounds HTS12673, BTB02076, and JFD00311 which showed important results with respect to all properties such as estimated activity, calculated drug-like properties and better GOLD fitness scores can be proposed as potential leads. Novelty search using SciFinder Scholar and PubChem compound search has also ascertained that these hits were not reported earlier for chymase inhibition.