By analyzing our built homology model, besides the transmembrane topology and secondary structure which is constant to the structure of 1NEK, we also found that an overall total of 80% of the polypeptide sequences of KPN00728 and KPN00729 established helices. A bunch of eight helices made up from four helices in KPN00728 mGluR and KPN00729, respectively are found. Along the secondary structure is about 40 A. This enable the structure to integrate into the membrane bilayer, which generally is within a thickness of 30 A. Additionally to this, we noticed signicant presence of amino acid residues such as Val and Leu in the product, situated quite close to the transmembrane region just like the observation described elsewhere. In terms of hydrophobicity, there’s more than 50 and 40% of amino acid residues in both KPN00728 and KPN00729, respectively which are hydrophobic. This is in agreement to the general rules of the transmembrane protein structure, where multiple helices with hydrophobic quality on the outer side are crucial for the string to its stability as well as to anchor on the membrane. Furthermore, sequence analysis buy Dinaciclib showed the current presence of conserved residues such as for instance Ser and Arg from Chain C and Tyr from Chain D of Succinate dehydrogenase take part in the binding of ubiquinone from other organisms. They are also found to be found near one another inside our model. Both His deposits from KPN00728 and KPN00729 were found to set up themselves in nearly axial place allowing the Heme group to sit comfortably between them. Furthermore from our molecular docking result, the synthesis of hydrogen bonds between ubiquinone with both proteins support our postulation of KPN00728 as the chain C and further demonstrated that KPN00729 is in fact Chain N of Succinate Eumycetoma dehydrogenase in Klebsiella pneumoniae MGH 78578. Additionally, they’ve high sequence identity with Succinate dehydrogenase from other organisms. From the analysis, we were able to nd the conserved residues within the lost area that is crucial for ubiquinone binding. The analysis of the developed homology design showed an agreement with the secondary structure prole of the Chains C and D of the enzyme undoubtedly tell us that both proteins are indeed section of Succinate dehydrogenase. this protein continues to be classied as hypothetical protein all in pan Akt inhibitor all, the missing genomic location of KPN00728 is possibly the most critical reason. Addition of this place in the protein, recognized by all the sequence analysis and molecular modeling results, has produced conclusive evidence that it’s in place Chain C of Succinate dehydrogenase. In this work, a variety of architectural modeling, protein sequence analysis, genome analysis and molecular docking simulation approaches were used to offer an understanding of the characteristics and possible functions of hypothetical proteins with not known structure and biochemical function.