Human papillomavirus infection is the cause of cervical cancer. The majority of human papillomavirus (HPV) infections are benign and resolve on their own. However, there is a risk of chronic infection with high-risk strains of HPV. Human HPV turns on the E6AP ubiquitin-protein ligase (E3), which makes it easier for the p53 tumor suppressor protein to break down in cervical cancer. The p53 tumor suppressor protein is a governing protein that inhibits tumorigenesis by regulating cell division and facilitating DNA repair mechanisms. The p53 protein resides in the nucleus of cells across the organism. Human malignancies often display this mutation, which may confer resistance to oncological therapies. A third type of enzyme, called an E3 ubiquitin-protein ligase, takes ubiquitin from an E2 ubiquitin-conjugating enzyme as a thioester and moves it to its target proteins. In this study, we prepared the protein and potential ligand molecules for molecular docking studies. We also applied computational strategies to demonstrate the pharmacokinetic properties in five different stages of the selected ligands that describe the drug's journey through the body. The objective of this study is to identify nature-derived compounds that have the ability to inhibit the E6AP-UbcH7 protein complex. These compounds have the potential to inhibit the harmful effects of HPV on the p53 tumor suppressor in cervical cancer. After performing docking between the ligand molecules and the receptor protein molecule, we determined the molecular docking scores. We found that kaempferol required the least energy to interact with the protein (docking score of -5.896 kcal/mol). The molecular docking and ADMET test results indicate that kaempferol is the most promising therapeutic candidate compared to the other compounds.