Aminoacyl -tRNA synthetases catalyze the attachment of amino acids to their specific tRNAs in protein synthesis. In higher eukaryotes several of these enzymes are found in a multienzyme complex. Jeong et al. solved the NMR structure of multifunctional peptide motifs in human bifunctional glutamyl-proyl-tRNA synthetase. To understand the motional properties and mode of action of the human bifunctional glutamyl-proyl-tRNA synthetase, molecular dynamics simulation of human bifunctional glutamyl-proyl-tRNA synthetase, in aqueous environment was carried out using the software, GROMACS. From the time evolution, Root Mean Square Deviation (RMSD), Root Mean Square Fluctuation (RMSF) and Radius of gyration (Rg), it was found that the toxin was relatively flexible. Principal Component Analysis (PCA) was also performed for better understanding of motional properties in reduced dimension. All these observations help us to understand the structure and function of human bifunctional glutamylproyl- tRNA synthetase.