MOLECULAR DOCKING STUDIES ON CYTOCHROME C IMMOBILIZED MESOPOROUS FE(III)-PHOSPHATE
Abstract
The results of molecular docking study on Cytochrome immobilized mesoporous Fe(III)-phosphate (FePO) using Autodock4.2software is described. The non-covalent i.e., supramolecular interactions of a high-resolution three-dimensional structure of horse heart cytochrome C, (PDB_ID 1HRC) with the monomeric (M1) and polymeric structure (M2) of mesoporous FePO units are deduced along with the binding energies. The results visualized the preferential binding orientation between the amino acid side chains of Cytochrome C and the phosphate units of M1/ M2 structures assisted by various supramolecular interactions, specifically hydrogen bonding, hydrophobic interactions at low pH conditions (Figure 1 and 2). Molecular docking of monomeric FePO ‘M1’ on Cytochrome C without Heme molecules in the active site was also constructed to understand the interactions (Figure 3).