Acinetobacter baumannii is a ubiquitous Gram-negative bacillus bacterium that is frequently found in the nosocomial infections. Regard to the rapid development of resistance against various antimicrobial agents due to the high ability of natural genetic transformation, A. baumannii is resistance to many of the antibiotics. Toxin-antitoxin system is one of the virulence agents in A. baumannii that can be involved in the emergence of drug resistance. HicB as a toxin system is an ideal target for the design of new classes of antimicrobial agents against A. baumannii. The goals of this work was to model the complete tridimensional structure of the HicB protein using computational methods and to assess structural and functional of it. The consistency of modeled structure was confirmed by different servers to high accuracy for modeling and dynamics simulation. The molecular dynamic simulation and virtual screening results indicate that HicB is a stable protein from A. baumannii. These results provide new insights for the molecular understanding and development of new antibacterial drugs against toxin system involved in A. baumannii pathogenesis.