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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7XJH

Isoproterenol-activated dog beta3 adrenergic receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
A0003091biological_processrenal water homeostasis
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007190biological_processactivation of adenylate cyclase activity
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007192biological_processadenylate cyclase-activating serotonin receptor signaling pathway
A0007608biological_processsensory perception of smell
A0010854molecular_functionadenylate cyclase regulator activity
A0010856molecular_functionadenylate cyclase activator activity
A0014819biological_processregulation of skeletal muscle contraction
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031748molecular_functionD1 dopamine receptor binding
A0032588cellular_componenttrans-Golgi network membrane
A0046872molecular_functionmetal ion binding
A0046907biological_processintracellular transport
A0048589biological_processdevelopmental growth
A0050796biological_processregulation of insulin secretion
A0050890biological_processcognition
A0060348biological_processbone development
A0060789biological_processhair follicle placode formation
A0070062cellular_componentextracellular exosome
A0070527biological_processplatelet aggregation
A0071377biological_processcellular response to glucagon stimulus
A0071380biological_processcellular response to prostaglandin E stimulus
A0071468biological_processcellular response to acidic pH
A0071870biological_processcellular response to catecholamine stimulus
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
A0097700biological_processvascular endothelial cell response to laminar fluid shear stress
A0120162biological_processpositive regulation of cold-induced thermogenesis
B0001750cellular_componentphotoreceptor outer segment
B0001917cellular_componentphotoreceptor inner segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0008283biological_processcell population proliferation
B0010659biological_processcardiac muscle cell apoptotic process
B0030159molecular_functionsignaling receptor complex adaptor activity
B0030425cellular_componentdendrite
B0030507molecular_functionspectrin binding
B0042622cellular_componentphotoreceptor outer segment membrane
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071456biological_processcellular response to hypoxia
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
R0004930molecular_functionG protein-coupled receptor activity
R0004935molecular_functionadrenergic receptor activity
R0004939molecular_functionbeta-adrenergic receptor activity
R0004993molecular_functionG protein-coupled serotonin receptor activity
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0007268biological_processchemical synaptic transmission
R0015052molecular_functionbeta3-adrenergic receptor activity
R0016020cellular_componentmembrane
R0030425cellular_componentdendrite
R0030594molecular_functionneurotransmitter receptor activity
R0042803molecular_functionprotein homodimerization activity
R0043235cellular_componentreceptor complex
R0043410biological_processpositive regulation of MAPK cascade
R0045202cellular_componentsynapse
R0051380molecular_functionnorepinephrine binding
R0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
R0098664biological_processG protein-coupled serotonin receptor signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCALAVDRYLaV
ChainResidueDetails
RALA123-VAL139
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues17
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04896","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues29
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues30
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-07-16

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