Homology Modeling, Docking Studies and Functional Site Analysis of Various Accessory Interacting Proteins of MnSOD of Nostoc PCC7120 and FeSOD of Thermosynechococcus elongatus

Antioxidant enzymes studies have been evolved to be a potent area of study in context to bioinformatics tools. These antioxidant enzymes are produced by the cell to scavenging the stress effect of and external stimuli. In context to the present study, FeSOD and MnSOD have been investigated using bioinformatics tools. The complex biological systems and their behaviours have now become easy to study via the available bioinformatics tools. Homology modelling has emerged as a powerful tool in predicting an unknown structure of a protein and through phylogenetic analysis we can predict a relationship between the two species of cyanobacteria taken in our current study. Modelling and molecular docking studies is an important step in systems biology study. Despite availability of hundreds of known protein sequences, accurate information about their role in pathways is still largely inaccurate. Here, an attempt is made to explore the structural and the interactions of the accessory proteins with the two enzymes viz. MnSOD (from Nostoc sp. PCC7120) and FeSOD (from Thermosynechococcus elongates) based on the maps available from STRING database with the help of molecular docking studies.