Abstract
FNR (fumarate nitrate reduction regulator) is an important oxygen regulation protein, which plays a major role in altering gene expression between aerobic and anaerobic conditions. In this study, the tertiary structure of FNR protein in Klebsiella pneumoniae was established using homology modelling. The model was modified and optimized using molecular mechanics and molecular dynamics simulations. In addition, Support Vector Machines (SVMs) was applied to predict the possible binding sites patches of FNR. The residues conservations were further analyzed and it was found that the Asn138-Ser162 region of FNR protein was the putative dimerization interface.
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