This computational study aims to understand the role of 2-deoxy-D-glucose as an antiviral and glycolysis pathway inhibitor in SAR-CoV-2 affected human body using PRinMTML-ESS platform. Using this platform molecular docking, all-atom molecular dynamics simulations with enhanced free energy simulation was performed and screening was done in each stage using effective scoring algorithm. Here we have explored the inhibition property of 2-DG with the four SAR-CoV-2 viral proteins 3CL pro , PL pro , NSp-16 and RdRp which are important for transmission and replication of SARS-CoV-2. 2-DG has very low dissociation barrier with O-methyl-transferase (Nsp16) and RdRp in free energy simulation. Hence it can be predicted that 2-DG can barely inhibit any viral protein taking part in replication and translation of SARS-CoV-2. On the other hand, PRinMTML-ESS platform predicts 2-DG binds strongly to hexokinase, the enzyme responsible for phosphorylation of glucose to glucose-6-phosphate in glycolysis. Though glucose has higher binding affinity to hexokinase, comparable binding affinity of 2-DG may lead to competitive inhibition of the glycolysis, hence the glycolytic flux is reduced which in turn reduces the replication and transcription of SARS-CoV-2 virus in human cells. Therefore, our study predicts that 2-DG though doesn't show any comparable inhibition for non-structured protein associated with translation and replication of SAR-CoV-2 can be used as a clinical therapy in COVID-19 infected patient for competitive inhibition of glycolysis process in virus infected cells, thereby reducing the rate the replication of virus.