Formate dehydrogenase from Acetobacteriumium woodii is under investigation for industrial conversion of CO2 to formate. To have an economically viable biotechnological process for production of formate from CO₂ the conversion rate needs to be increased substantially. Here, we used structure prediction and molecular modelingfor predicting a reliable 3D structure of A. woodii FDH and following docking experiments we identified two critical residues as main formate binding sites in the enzyme. Our result will help to increase the efficacy of CO₂ fixation as a biotechnological approach to reduce the atmospheric concentration of this greenhouse gas as well as biologically producing formate as a safe way of H2 transport in biofuel application.