ATP-triggered drug research is a targeted drug delivery method in which drugs are released in response to elevated ATP levers. Higher ATP levers are common in tumors and inflammatory tissues. The drug is entrapped in a nano vehicle and with an ATP-response element such as aptamers. A higher ATP concentration makes structural changes in the aptamer and releases the drug in a precise location. The nanovehicle-targeted drug transport mechanism heavily depends on the structure of the aptamer. Therefore, we have predicted the aptamer 3D structure for both ATP aptamer (present inside the nanovehicle) and HB5 aptamer (present on the surface). The ATP aptamer is smaller and circular with only 27 base pairs and helps bind ECGC and protamine. On the other hand, the HB5 aptamer is an 86-base pair long and linear shape aptamer that binds to the HER2 receptors present in abundance on the cancer cell's surface. The linear and long shapes are essential for aptamer to extend and bind to the HER2 receptor. Molecular docking shows that the HB5 interacts with the binding site on the HER2 receptor, further confirming our results. The HB5 receptor's Lenier orientation will let it attach to the HER2 receptor head-on. "Head-on" describes how the HB5 aptamer directly and linearly binds to the HER2 receptor, strengthening the nanovehicle's adherence to cancer cells for efficient drug delivery. For the best possible binding and therapeutic effectiveness, this orientation is essential. Nevertheless, docking simulations demonstrate that the HER2 receptor is vertically bound by the control receptor. As a result, the Her2 receptor and the control receptor are unable to interact correctly. These results also show that a head-on binding between aptamer and HER2 receptor is essential for the nanovehicle binding to the cancer cell's surface.