Snake venom contains a diverse array of pharmacologically active proteins and polypeptides that have led to the development of molecular probes and therapeutic agents. Short neurotoxins and cytotoxins are non-enzymatic polypeptides components of snake venom found only in the venoms of Elapidae (cobras, kraits, mambas, coral snakes and Australian elapids) and Hydrophidae (sea snakes). The three-dimensional structure of short neurotoxins and cytotoxins has three beta stranded loops resembling three-fingers of three-finger protein super family. This protein super family has different family members which are employed in various biological functions. The objective of this study is to search out the amino acid compositional (%) profile, physiochemical properties and functional analysis of three finger toxins present in different elapid snake species to be precise, Bungarus fasciatus, Naja naja and Naja kauthia. We analyzed a total of 23 reference protein sequences representing short neurotoxin and cytotoxin of three elapid snakes and related non-toxin proteins of human in terms of functional analysis, amino acid compositional (%) profile, number of amino acids, molecular weight, theoretical isoelectric point (pI), number of positively charged and negatively charged amino acid residues, instability index and grand average of hydropathy using computational tools. From the result it was found that amino acid composition profile represents that all sequences hold a conserved cysteine amount even as differential amount of different amino acid residues have a particular family pattern. It will also assist to know about involvement in various biological functions those are accountable for the vivid amino acid composition profile of these proteins. This comparative analysis of physicochemical properties would play a significant role in understanding the mechanisms of action of toxins and in the development of lead therapeutic molecules.