Cardiolipin, a type of phospholipid, is naturally produced within the mitochondrial membrane. It was initially discovered in animal hearts and is predominantly located on bacterial membranes. Several research has been made to understand the structure and function and their role inside the mitochondrial membrane. In this study, we present accurate details regarding the CL binding residues for various organisms namely Bos Taurus, Mus Musculus, Cereibacter sphaeroides and Methanosarcina acetivorans. To achieve this, we developed a Python program specifically designed for CL binding. We extracted data from the Protein data bank. The results show that polar aliphatic positively charged amino acids are highly preferred in CL. The structure of the binding residues with lipid was visualized with the help of the AVAGADRO tool.
