Mucin 1 (MUC1) is a membrane-bound glycoprotein that is present on the apical surface of epithelial cells. A lot of studies have connected it to epithelial adenocarcinomas growth, metastasis, and poor prognosis. Carbohydrate groups' numerous structural alterations associated with the protein backbone are one of the qualitative alterations in MUC1 during epithelial adenocarcinoma. Importantly glycan structures play a crucial function in the cellular connection. Here in this study, we constructed 3D MUC1-VNTR structure and Core 1-4 were added to their appropriate locations thereby designed MUC1Wild type and MUC1Cancer . Different bioinformatics analysis such that Root Mean Square Deviation, Root Mean Square Fluctuations, Radius of Gyration, Hydrogen bonding, Secondary Structure Determination, Clustering, and Principal Component analysis was performed on the 100 ns molecular dynamic simulation trajectories. We found out that RMSD, RMSf, and Rgyr significantly differ between the MUC1Wild and MUC1Cancer. More H-bonding and strong protein stability and folding were seen in the MUC1Wild and PCA analysis further confirms MUC1Wild compact motion in the parallel direction during MD simulation. These research findings revealed structural dynamics of the MUC1Wild and MUC1Cancer VNTR Mucin1 areas that could not be investigated experimentally, allowing us to build a more complete picture of their carcinogenic effects. Furthermore, glycation differences in protein structure can impact the overall conformational interaction network and give structural insight for drug discovery and biomarker development.