Of several ALH-driven QS found in different organisms such as P. aeruginosa, P. putida, Chromobacterium violaceum, Escherichia coli, Proteus mirabilis, Serratia marcescens, Agrobacterium tumefaciens, Erwinia carotovora and Yersinia enterocolitica, the LasR-induced activation is most widely studied and can be considered as model pathway to study this type of QS [3]. However, till date no LuxR-mediated QS inhibition by QSI is reported in bioluminescent Vibrio. LasR and LuxR possess great deal of similarity, of which, one being the most widely studied and the latter to be least studied for QSI, both these proteins were accessed for QUI assessment under present study. LasR crystal structure is also available whilst that of LuxR is not available; therefore, building the 3D structure using homology modelling was imperative. Choosing the correct 3D template for LuxR structure building becomes a vital step. Nasser and Reverchon [6] have vividly described the family of Lux-like proteins involved in QS mechanism from different microbes and concluded that LuxR protein sequence showed maximum homology with TraR from A. tumefaciens. The crystallized 3D structure is available in PDB and the structure with PDB ID 2q0o was used to build the LuxR model. To analyse the quality of the model build, QMEAN4 and QMEANDisCo, ERRAT and Ramachandran plot were analysed using MolProbity. The results obtained showed the quality of the model built was at par with the parameters for homology modelling published so far [24].