Chickpea is an important crop legume and presently gains extensive scientific importance for their agroeconomic, nutritional as well as medicinal properties. The production of this important crop is seriously challenged by Fusarium oxysporum for causing wilt disease. As a prevalent plant immune response chickpea plant produces reactive oxygen species (ROS) to counteract pathogens but the oxidative burst is detrimental to the plant itself. As a consequence, the plant also activates its antioxidant scavenging system, e.g., catalase to detoxify the harmful effect of ROS and generate ROS signatures for downstream signaling. Cicer arietinum catalase 4 (Ca catalase 4) is found to be induced significantly after pathogen attack in chickpea plants. The structural information of Ca catalase 4 is absent for chickpea plants. This study investigated the physio-chemical properties of the protein, the basic structure (secondary and tertiary) of Ca catalase 4, and its validation through various computational techniques. Interaction cavities present on the protein surface structure were also analysed. Finally, a protein–protein interaction network with the central activity of the catalase enzyme was predicted through Pathway Studio software. This study gives an insight into the structure of an important catalase enzyme for its future biotechnological application.