Human immunodeficiency virus 1 (HIV-1) infection is a slowly replicating retrovirus that leads to acquired immunodeficiency syndrome (AIDS). In this paper, the PDB file of gp120 and CD4 were obtained from the Protein Data Bank. The Expasy-ProtParam tool was used to analyze the physicochemical properties of HIV-1 gp120. ClusPro 2.0 was used to dock the interaction between gp120 and CD4. We described structural basis, affinity and kinetics of binding, and explored how CD4 cumulatively targeted most of the external surface of the envelope glycoprotein. These results showed that uncleaved gp120 had native-like structures and supported their used as candidate antibodies.