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Structure of a Protein Phosphatase 2A Holoenzyme with B55 subunit[HYDROLASE/HYDROLASE INHIBITOR]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
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Bovine GRK2 in complex with Gbetagamma subunits and a selective kinase inhibitor (CMPD103A)[TRANSFERASE/SIGNALING PROTEIN/INHIBITOR]
Bovine GRK2 in complex with Gbetagamma subunits and a selective kinase inhibitor (CMPD101)[TRANSFERASE/SIGNALING PROTEIN/INHIBITOR]
Bovine GRK2 in complex with Gbetagamma subunits[TRANSFERASE/SIGNALING PROTEIN]
View in iCn3D Similar StructuresPubMedProteinsConserved Domains
Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits[TRANSFERASE/HYDROLASE]
Structure of heterotrimeric G protein Galpha-q beta gamma in complex with an inhibitor YM-254890[SIGNALING PROTEIN/INHIBITOR]
Human GRK2 in complex with Gbetgamma subunits and balanol (co-crystal)[PROTEIN BINDING]
Human GRK2 in complex with Gbetgamma subunits and balanol (soak)[PROTEIN BINDING]
HETEROTRIMERIC COMPLEX OF PHOSDUCIN/TRANSDUCIN BETA-GAMMA[COMPLEX (TRANSDUCER/TRANSDUCTION)]
Human Grk2 In Complex With Gbetagamma Subunits[TransferaseSIGNALING PROTEIN, EC: 2.7.11.15]
BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN[COMPLEX (GTP-BINDING/TRANSDUCER)]
G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND[COMPLEX (GTP-BINDING/TRANSDUCER)]
Heterotrimeric Complex Of A Gt-AlphaGI-Alpha Chimera And The Gt-Beta-Gamma Subunits[Complex (Gtp-BindingTRANSDUCER)]
G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND[COMPLEX (GTP-BINDING/TRANSDUCER)]
The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer[SIGNALING PROTEIN]
Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits[TRANSFERASE]
STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA[SIGNALING PROTEIN]
STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN[SIGNALING PROTEIN]
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