The complete genome of MN908947.3 SARS-CoV-2 virus isolate Wuhan-Hu-1 encodes a 4409aa long protein along with the other glycoproteins and polyproteins. The homology modelling of this protein showed sequence and structural alignment with two SARS proteases with structural accession numbers 3e9s.1 and 2a5i.1 at positions 1568-1882 and 3268-3573 respectively. Reports suggests inhibition of virus replication by TTT ligand and an aza-peptide epoxide inhibiting the main peptidase. The structural similarity of these templates are 83% and 96% respectively. The multiple sequence alignment shows complete conservation of the sequence suggesting a high degree of homology. The protein ligand interaction analysis of the Novel Coronavirus non structural protein and papain-like protease is shown in Fig. . The Comparison of Hydrophobic interaction, hydrogen bonding, salt bridges of the constructed model of the Novel Coronavirus protein from region 3268-3573 aa to ligand AZP with Hydrophobic interaction, hydrogen bonding, salt bridges of the template 2a5i is given in Suppl. Table , when comparing both it is seen that the binding properties are the same expect for the presence of water bridge in the template 2a5i.