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TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST SALBUTAMOL[RECEPTOR]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST ISOPRENALINE[RECEPTOR]
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST CARMOTEROL[RECEPTOR]
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB102)[RECEPTOR]
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND PARTIAL AGONIST DOBUTAMINE (CRYSTAL DOB92)[RECEPTOR]
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CYANOPINDOLOL[RECEPTOR]
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST IODOCYANOPINDOLOL[RECEPTOR]
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CARAZOLOL[RECEPTOR]
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL[RECEPTOR]
Crystal structure of the beta2 adrenergic receptor-Gs protein complex[SIGNALING PROTEIN/Hydrolase]
Crystal structure of a Methylated beta2 Adrenergic Receptor-Fab complex[SIGNALING PROTEIN]
Structure of a nanobody-stabilized active state of the beta2 adrenoceptor[SIGNALING PROTEIN, Hydrolase]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
Crystal structure of the human beta2 adrenergic receptor in complex with the neutral antagonist alprenolol[MEMBRANE PROTEIN]
Crystal structure of the human beta2 adrenergic receptor in complex with a novel inverse agonist[MEMBRANE PROTEIN]
Crystal structure of the human beta2 adrenergic receptor in complex with the inverse agonist ICI 118,551[MEMBRANE PROTEIN]
Cholesterol bound form of human beta2 adrenergic receptor[MEMBRANE PROTEIN]
Irreversible Agonist-Beta2 Adrenoceptor Complex[Membrane Protein/Hydrolase]
Substance P in isotropic q=0.25 DMPC/CHAPS/GM1 bicelles as a ligand for NK1R[NEUROPEPTIDE RECEPTOR/NEUROPEPTIDE]
Substance P in DMPC/CHAPS isotropic q=0.25 bicelles as a ligand for NK1R[NEUROPEPTIDE RECEPTOR/NEUROPEPTIDE]
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