Berovin is a Ca2+- binding photoprotein from Beroe abyssicola that belongs to the CTENOPHORES group. A comparison of the two most famous groups of calcium-regulated photoproteins, Coelentrates and CTENOPHORES, showed high degree of structural similarity regardless of their low sequence identity. Up to now, the crystal structures of several photoproteins such as aequorin, obelin have been solved. Based on these crystal structures, a mechanism have been proposed to explain how Ca2+ binding might trigger the bioluminescence reaction in Coelentrates group. The side chains of His175 and Tyr190 along with the Trp179 in obelin are in close vicinity to the peroxy group of 2-hydroperoxy coelenterazine implying strong hydrogen bonds between them. It was suggested that the His-Trp-Tyr triad participates in stabilization of the 2-hydroperoxy derivative of coelenterazine and might be involved in some steps of the bioluminescence reaction. Despite the precise investigation of Ctenophore binding site, sequence alignment between Coelenterates and CTENOPHORES group and mutagenesis studies on berovin and mnemiopsin, we could not obtain its catalytic triad. This result refers to this point that another light emission mechanism can be existed in CTENOPHORES group. In this study, the localization of coelentrazine in photoprotein of berovin was investigate by docking study. We optimized the full structure of berovin resulting from docking simulation by molecular dynamics simulation. At the optimized conformation, the interactions between amino acids of cavity and the ligand were examined. The results showed that the coelentrazine was located in protein structure with different orientation compared with other Coelentrates photoproteins.