Currently, 60% of all drugs in the market bind to G-protein coupled receptors (GPCR)¹. Among GPCRs, adenosine-subtype A2B has raised interest because it is related to diseases such as cancer and sickle cell disease². However, this target doesn’t have a crystallographic structure available. Thus, we built the receptor 3D model on SWISS-Model server3(template PDB:5IU7; 60.26% identity) with adequate structural parameters: GMQE (0.75) and QMEAN(-3.12). Through CHARMM-GUI server, we inserted it into a lipid membrane and ran a molecular dynamics (MD) simulation on GROMACS 5.1.24: CHARMM forcefield; pH=7.4; NVT; T=303.15K; t=100ns. We compared the stability of our systems: A2B and A2B-antagonist. The deviation and fluctuation data were: 3.14x10-1± 5.81x10-2nm (A2B) and 1.61x10-1± 5.31x10-3nm (A2B-antagonist) and 1.11x10-1± 8.45x10-2nm (A2B) and 6.89x10-2± 2.61x10-2nm (A2B-antagonist). The antagonist stabilizes binding-site residues when compared to the A2B form, making the system reliable to be used in next virtual screening steps to identify new promising A2B antagonists.