The cation-π interactions are necessary for molecular recognition in biological receptors. Here, in this study we have analyzed the energy contribution of cation-π interaction in the coagulation cascade pathways proteins with 'A' chains of their PDB structure. The contribution of cation-π interacting residues in stabilizing residues and centres, secondary structure, solvent accessibility and conservation score has been well studied. With total data set of 190 proteins, 160 showed significant cation-π interactions. Cation-π residues pair's involved Arg-Tyr pair and showed maximum number of cation-π interactions and Lys- Try residue pair showed minimum interactions. The cation-π interaction energy depicted that Arg-Tyr showed high energy and Lys-Tyr showed less energy. In the secondary structure, Arg and Lys preferred to be in strands because of Phe in coil and Try in helix. Residues Arg and Lys preferred to be in exposed region and π residue Phe preferred buried regions of the proteins. The significance of cation-π interaction in the stability of therapeutic proteins and pharmacology studies is important.