a-Glucosidase is an important biocatalyst in carbohydrate metabolism by hydrolyzing disaccharide into glucose. This enzyme crucially regulates postprandial blood sugar levels. Hence, these features positioned it as a possible target for diabetes therapy and highlight its relevance for therapeutic purposes. But conventional experimental techniques are not adequate for a thorough understanding of the structural and dynamic characteristics of the enzyme at the atomic level and thus frequently lack the capacity to characterize those protein conformational changes that are required for function. Here, we performed MD simulations to explore the structural and dynamic properties of a-glucosidase on an atomistic level. The analyses suggested that a delicate balance exists between rigid core regions, which maintain enzyme integrity, and dynamic surface regions, most notably near the active site. It was also observed that residues within the core structure of enzyme were highly stable. and key molecular interactions, such as hydrogen bonds and salt bridges, were shown to play a vital role to maintain structural integrity. Furthermore, dynamic residues and regions have been identified necessary to bind substrates and inhibitors. In conclusion, the findings of the study provide valuable insights into the functional dynamics of a-glucosidase and hence they can help deepen our understanding of its role in metabolic diseases. In this regard, the obtained outcomes can not only enhance the basic understanding of a-glucosidase structure-function relationship, but they can also pave the way for the design of new therapeutic strategies in diabetes and associated pathologies.