The phenomenon of receptor bias refers to the selective signaling through a GPCR, mediated by either G protein or β-arrestin, due to mutations. Investigating thefunctional dynamics of biased receptors holds significant potential in elucidating the fundamentals of transducer selective signaling in GPCRs induced by biased ligands. In β2AR, a single mutation (Y2195.58A) selects against GRK binding, thus, disfavoring the association with β-arrestins, leading to G protein bias of the receptor.18 Whereas, a triple mutation (T682.39F, Y1323.51G, and Y2195.58A) inhibits G protein signaling, consequently resulting in β-arrestin bias.17 In an attempt to understand the atomistic basis of this biased signaling in β2AR, we performed large-scale all-atom enhanced sampling GaMD simulations and analyzed the allosteric conformational changes sampled by mutant receptors.Our observations reveal specific conformations of the transmembrane helices in the extracellular and cytosolic regions of the mutant receptors compared to the wild-type. In the single mutant, ICL3 mostly positions away from the transducer-binding cavity, sampling an open state that facilitates G protein binding. In contrast, the triple mutant prefers a closed state of the ICL3, thereby occluding the cavity for G protein engagement. Further, in the mutant receptors, the side chains of R1313.50 and Y3267.53 in the conserved motifs D(E)RY and NPxxY exhibit characteristic orientations that could enable specific transducer interactions. In particular, the β-arrestin-favoring triple mutant displays a relatively larger population of the downward rotameric state of R1313.50, characterized by a cytoplasm-facing side chain conformation that selectively facilitates the engagement of β-arrestin over G protein. By employing machine learning classification algorithms, we discern the inter-residue interactions that promote different orientations of R1313.50 and Y3267.53 in the wild-type and mutant systems. The evaluation of suboptimal paths reveals distinctive rewiring of allosteric communication pathways between the extracellular agonist BI-167107 and the residues in the interfaces of various transducers (G protein and GRK/β-arrestin). These allosteric reconfigurations drive specific conformational sampling, resulting in the selective engagement of transducers in both single and triple mutants. The critical residues identified in allosteric signal transfer for each β2AR mutant present promising opportunities for future experimental and computational investigations that could target the sites to unravel the allosteric mechanisms underlying biased signaling across various other GPCRs. Moreover, the atomistic insights presented here may help in developing therapeutic strategies for diseases caused by mutations in GPCRs and aid in designing biased drugs that target these receptors with fewer side effects and better efficacy.