Nipah henipavirus is an emerging RNA virus that poses a danger to world safety due to its high fatality rate. The Nipah virus has caused several illness epidemics in South and Southeast Asia. The matrix protein of Nipah henipavirus plays a crucial function in linking the viral envelope to the virus core. Connecting the viral envelope to the virus core is critical for virus assembly. Through analyses of structural and functional protein explanations, bioinformatics tools can aid in our comprehension of the protein. This study intends to provide structural and functional annotations to proteins. Using in-silico approaches, the analysis also assigns the protein's physicochemical properties, three-dimensional structure, and functional annotation. The in silico research validated the protein’s hydrophilic nature and alpha (α) helix-dominated secondary structure. The protein's tertiary structure model is generally consistent based on various quality evaluation approaches. The functional explanation claimed that the protein is a structural protein that connects the viral envelope to the virus core, a protein that is necessary for virus assembly. This study reveals the importance of the matrix protein as a functional protein needed by Nipah henipavirus.