Objective: To analyze the structural features of human P2X7R protein, meanwhile homology, protein- protein interaction, and cell epitope were predicted to provide theoretical basis for the diagnosis and treatment of related diseases. Methods: Human P2X7R protein was analyzed and predicted by ProtParam、TMHMM、ProtScale and SignalP 5.0 Server et al. Results: Human P2X7R protein is composed of 595 amino acids, the molecular formula is C 3077 H 4749 N 835 O 871 S 40, with the theoretical isoelectric point PI of 8.62, the instability coefficient is 46.07, the total average hydrophilicity is -0.317, and the protein is an hydrophilic protein instead of secreted protein, no any signal peptide, but transmembrane region is contained, which belong to transmembrane protein. There are 157 α helices and 288 random coils in the secondary structure of human P2X7R protein, accounting for 26.39％ and 48.40％ of all amino acids, The coverage rate of the three-level structure prediction results is 100％, and the sequence consistency is 80.34％, and the ramachandran plot show that the predicted structure is relatively stability. The interaction of proteins show that there are a variety of proteins interacting with human P2X7R, and P2X7R was closely related to inflammation; this protein had many B and T cell epitopes, which could provide ideas for vaccine development. Conclusion: The results indicate that the analysis of human P2X7R protein that is based on bioinformatics method has certain reliability. P2X7R is involved in the development of inflammatory diseases, and the antigenic epitope of B, Th and CTL cells screened out by prediction will provide the treatment scheme for diseases.