Molecular docking as a computational tool for analyzing product mediated inhibition for ß-galactosidase immobilized on glutaraldehyde modified matrices

Abstract

Chemical informatics aims to disseminate information regarding the design and structure of a compound for revealing chemical information of a target with the help of molecular modeling/simulation. Hence, in the present study, efforts were raised to analyze the ligand interaction plots of glucose and galactose for Aspergillus oryzae ß-galactosidase. The crystallographic structure of enzyme was obtained from protein data bank ID: 4IUG while the 3D structure of glutaraldehyde was obtained from PubChem with compound ID 3485. It was prepared by Chimera v.1.6.2 for hydrogen and charge addition. Chimera v.1.6.2 and PyMOL v.1.3 were used for visual analyses and illustration of protein-ligand complex. The ligand interaction plots of protein-ligand complexes were illustrated by Ligplot+ v.1.4.5 program. Enzyme showed optimum binding affinity on a molecular target with the binding energy of -9.5 kcal/mol.