Pulsed electromagnetic fields (PEMFs) are increasingly used in clinical settings for the treatment of inflammatory and degenerative conditions. Among their molecular targets, \(\hbox {A}_{2A}\) adenosine receptors (\(\hbox {A}_{2A}\hbox {ARs}\)) show increased receptor density on the cell membrane upon PEMF exposure, yet the underlying physical mechanism remains uncertain. In this study, atomistic molecular dynamics simulations were used to investigate how an external static magnetic field, used as a simplified representation of the quasi-static magnetic component of PEMF exposure, influences the structure and electrostatics of the \(\hbox {A}_{2A}\hbox {AR}\). Our simulations revealed that the field predominantly affects the receptor’s extracellular region, resulting in a transition from a closed to a more open conformation of the ligand-entry region. This structural rearrangement was accompanied by widening and increased hydration of the extracellular entrance, indicating enhanced accessibility of the orthosteric binding site. At residue level, Glu169, Ala265, and Pro266 exhibited pronounced dipole reorientation, indicating localized electrostatic adaptation consistent with the structural response. Together, these findings provide an atomistic insight into how magnetic perturbations can influence \(\hbox {A}_{2A}\hbox {AR}\) extracellular dynamics and offer a mechanistic framework compatible with experimental observations of altered \(\hbox {A}_{2A}\hbox {AR}\) function under PEMF exposure.
