Beta2 adrenergic receptor β₂ AR) is one member of G protein coupled receptors (GPCRs), which is a key pharmaceutical target in the treatment of asthma. Evolutionary trace (ET) method was employed to analyze AR sequences and 44 conserved residues were identified. Then molecular dynamics (MD) simulation of the β₂ wild-type receptor, D130N active mutant and D79N inactive mutant were carried out and tried to explore the structural/dynamic features characterizing functionally different states of the receptor, by means of investigating ET identified conserved basic residues in the wild-type receptor and its two mutants. Particularly, it was found that the departing of D130 from R131 of DRY motif and approaching to K149 are highly correlated with the receptor activation, and the movement of helix 2, 4 and 6 upon receptor activation is inferred from the observation that R151 and K270 interact with other residues in the receptor active state on the basis of little change of the side chain orientations. The results might provide further insights into the activating mechanism of β₂ AR mutants, as well as the molecular bases of the diseases induced by the mutations of the receptor.