By studying our designed homology design, form transmembrane topology and secondary structure which can be constant to the structure of 1NEK, we also found that an overall total of 80% of the polypeptide sequences of KPN00728 and KPN00729 formed helices. A bundle of eight helices composed from four helices in KPN00728 mGluR and KPN00729, respectively are located. Along the secondary structure is about 40 A. This enable the design to incorporate into the membrane bilayer, which in general is at a depth of 30 A. Furthermore to this, we observed signicant existence of amino acid residues such as for example Leu and Val in the design, located quite close to the transmembrane region similar to the statement noted elsewhere. When it comes to hydrophobicity, there is 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 framework, where multiple helices with hydrophobic characteristic on the outer side are crucial for the chain to anchor on the membrane as well as to steadfastly keep up its security. More over, sequence analysis FAAH inhibitor showed the current presence of conserved residues such as Ser and Arg from Chain H and Tyr from Chain N of Succinate dehydrogenase take part in the binding of ubiquinone from other organisms. They’re also found to be located near to each other inside our model. Both His elements from KPN00728 and KPN00729 were found to prepare themselves in almost axial place enabling the Heme team to sit comfortably between them. Furthermore from our molecular docking result, the synthesis of hydrogen bonds between ubiquinone with both proteins help our postulation of KPN00728 because the chain C and further shown that KPN00729 is in fact Chain N of Succinate Lymphatic system dehydrogenase in Klebsiella pneumoniae MGH 78578. In addition, they have substantial sequence identity with Succinate dehydrogenase from other organisms. From the genome research, we managed to nd the conserved residues within the lost place which is critical for ubiquinone binding. The analysis of the developed homology product showed an agreement with the secondary structure prole of the Chains C and D of the molecule truly convince us that both proteins are indeed element of Succinate dehydrogenase. All in CDK7 inhibitor all, the lost genomic location of KPN00728 is probably the most critical reasons why this protein continues to be classied as hypothetical protein. 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 effect Chain C of Succinate dehydrogenase. In this work, a variety of architectural modeling, protein sequence analysis, genome analysis and molecular docking simulation strategies were employed to supply a knowledge of the possible functions and faculties of hypothetical proteins with not known structure and biochemical function.