The conformational changes of protein complex were also analyzed by MD simulations in terms of Principal components analysis, where we have taken into consideration of the first eigenvectors, to trace down the movement of macromolecule. Pczdump was used to prepare the average coordinates from simulation and was used to show the projections of eigenvectors. The approach helps us in correlating the related fluctuations of protein atoms with that of the total fluctuation in the course of simulation. Fig. 3b represents a porcupine plot for backbone atoms and the red spikes represent the directionality regarding the Clopidol motional behavior. The structural regions those are in contacts at the interface both of the proteins are shown an enclosed box in Fig. 3b. We also analyzed the polar contacts formed between these two proteins, by analyzing the coordinate files at regular interval from MD trajectory, though the numbers of hydrogen bond remains same but the residues participating varies. An overview of the residue pairs that are in contact, had been generated based upon the average structure and is represented by Contact-map in Fig. 5. Thus, the fundamental observation as found from the simulation study, being the hydrophobic forces, i.e. the Van der Waals interaction plays crucial role in making the protein complex stable, even in the explicit solvent conditions. Interestingly, in vitro assembly and transfer of Fe-S clusters on these P-loop NTPases did not required nucleotide binding or hydrolysis. However, in yeast, nucleotide binding and hydrolysis are required for Fe binding to Cfd1 and Nbp35 in vivo. The C-terminal domain of scNbp35 holds a 4Fe-4S cluster. The mutational study on scCfd1 and scNbp35 proteins has shown that two central cysteine residues of the C-terminal motif are crucial for the co-ordination of the labile clusters and the formation of the PF-4981517 Cfd1Nbp35 hetero-tetramer complex formation, and the viability of the yeast cells. Nbp35 has the capacity to bind a ferrodoxin-like cluster at the N-terminus of each monomer and a single cluster bridging a Nbp35 dimer through the conserved CX2C motif near the C-terminus of each monomer.