Newcastle Disease (ND) is caused by Newcastle Disease Virus (NDV) and is a major problem in developing countries where vaccination against NDV is not easily achievable. A step required for NDV infection is the cleavage of the NDV fusion (F) protein. Using structural information of the NDV F protein and the only known host protein binding partner, protein disulfide isomerase A3 (PDIA3), we computer modeled the interaction between the two proteins by looking at a docked structure of these two proteins. With our docked structure, we visualized one of the catalytic domains of PDIA3 being near the cleavage site of the NDV F protein. We also discovered a novel binding pocket on the NDV F protein that interacts with the second catalytic domain of PDIA3. This new insight may provide additional molecular targets for NDV vaccine development.