Prediction of enzyme-inhibitor interactions in avicennia marina Cu-Zn superoxide dismutase: implications of functionally significant residues in the metal binding sites

3D homology model of Cu-Zn superoxide dismutase from Avicemlia marina (AMSOD) was constructed using the structural coordinates of Spinach SOD (SSOD). Structural features of the model were outlined and correlated with respective functional aspects. Despite the similar overall fold, the homology model of AMSOD showed some distinct structural changes as compared to the template, SSOD. AM SOD was also modeled with specific inhibitors; azide, phosphate, thiocyanide and nitrite. Despite sequence variations, the inhibitor-enzyme interactions were quite similar. We also report some changes in the structure of AMSOD after mutation (P108D and H109Y) at the crucial sites. (author)