Cytochrome c peroxidase (Ccp1) is a mitochondrial heme-containing enzyme that has served for decades as a chemical model to explore the structure function relationship of heme enzymes. Unveiling the impact of its heme pocket residues on the structural behavior, the non-covalent interactions and consequently its peroxidase activity has been a matter of increasing interest. To further probe these roles, we conducted intensive all-atom molecular dynamics simulations on WT and nineteen in-silico generated Ccp1 variants followed by a detailed structural and energetic analysis of H₂O₂ binding and pairwise interactions. Different structural analysis including RMSD, RMSF, radius of gyration and the number of Hydrogen bonds clearly demonstrate that none of the studied mutants induce a significant structural change relative to the WT behavior. In an excellent agreement with experimental observations, the structural change induced by all the studied mutant systems is found to be very localized only to their surrounding environment. The determined interaction energies between residues and Gibbs binding energies for the WT Ccp1 and the nineteen variants, helped to identify the precise effect of each mutated residues on both the binding of H₂O₂ and the non-covalent interaction and thus the overall peroxidase activity. The roles of surrounding residues in adopting unique distinctive electronic feature by Ccp1 has been discerned. Our valuable findings have clarified the functions of various residues in Ccp1 and thereby provided novel atomistic insights into its function. Overall, due to the conserved residues of the heme-pocket amongst various peroxidases, the obtained remarks in this work are highly valuable.