Table 2.

The chemical structures of top six scoring ligand molecules against MLAA-42 protein.

S. no.	Structure and IUPAC name of molecule	Glide energy (KJ/Mol)	Binding energy (Kcal/mol)	The interacting amino acid residues	Bond distance (Å)
1		−63.59	−12.19	H-bonds
				LYS40 : N – L1	2.91
				THR98 : N – L1	2.50
				ILE100 : N – L1	2.67
				LYS40 : O – L1	2.32
				ILE96 : O – L1	2.18
				THR98 : O – L1	2.15
2		−50.27	−11.83	H-bonds
				TYR38 : N – L2	2.89
				ILE100 : N – L2	2.99
				TYR38 : O – L2	1.94
				π-π interactions
				TRP85-L2	4.95
3		−42.22	−11.61	H-bonds
				ILE100 : H – L3	1.68
				THR98 : O – L3	2.36
				TYR38 : O – L3	2.00
4		−47.52	−11.30	H-bonds
				LYS40 : N – L4	2.95
				THR98 : N – L4	2.65
				THR98 : O – L4	2.26
5		−39.53	−11.12	H-bonds
				LYS40 : N – L5	2.67
				THR98 : O – L5	2.13
				ASP99 : OD1-L5	2.79
				π-π interactions
				TRP85-L5	4.87
6		−40.65	−11.10	H-bonds
				ILE100 : N – L6	2.69
				TYR38 : O – L6	2.30
				THR98 : OG1-L6	2.29

Table represents top six ligand molecules with binding energies in range of −12.19 to −9.22 Kcal/mol, hydrogen bonds, and pi-interactions to MLAA-42's active site pocket.