Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9IJE

Epinephrine-activated human beta3 adrenergic receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003924molecular_functionGTPase activity
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
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
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007606biological_processsensory perception of chemical stimulus
A0010856molecular_functionadenylate cyclase activator activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031698molecular_functionbeta-2 adrenergic receptor binding
A0031748molecular_functionD1 dopamine receptor binding
A0031852molecular_functionmu-type opioid receptor binding
A0035255molecular_functionionotropic glutamate receptor binding
A0046872molecular_functionmetal ion binding
A0051430molecular_functioncorticotropin-releasing hormone receptor 1 binding
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
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
C0005834cellular_componentheterotrimeric G-protein complex
C0007186biological_processG protein-coupled receptor signaling pathway
C0031681molecular_functionG-protein beta-subunit binding
R0004930molecular_functionG protein-coupled receptor activity
R0004935molecular_functionadrenergic receptor activity
R0004939molecular_functionbeta-adrenergic receptor activity
R0007186biological_processG protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwTLCALAVDRYLaV
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 Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641
ChainResidueDetails
AGLY47
ALEU197
AASP223
ALEU292
APHE366

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715
ChainResidueDetails
ASER54
ATHR204

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
AHIS352
RARG179-PRO203
RARG315-PRO326

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
AASP300

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250
ChainResidueDetails
RTHR156-TRP178

site_idSWS_FT_FI6
Number of Residues21
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250
ChainResidueDetails
RTYR204-ALA225

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250
ChainResidueDetails
RTHR293-LEU314

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250
ChainResidueDetails
RALA327-CYS347

site_idSWS_FT_FI9
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250
ChainResidueDetails
RCYS361

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon