Adenosine A2A receptor (A2AR) is a G-protein coupled receptor that is involved in various physiological functions. Zeatin, a plant cytokinin and a derivative of adenine, is recently identified as new ligand of A2AR. However, the ligand-receptor interaction mechanism is not fully revealed. Here, we report a model structure of A2AR in complex with zeatin for the first time, to provide a better understanding of this interaction mechanism. A model structure of A2AR in complex with caffeine used as a positive control. As a result, zeatin displayed the ability to stay more stable at the binding pocket compared with caffeine and the residues involved in the interaction are identified. We propose that zeatin is indeed a novel and promising target for A2AR