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8UO3

CryoEM structure of beta-2-adrenergic receptor in complex with GTP-bound Gs heterotrimer (Class S)

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0007608biological_processsensory perception of smell
A0010856molecular_functionadenylate cyclase activator activity
A0016020cellular_componentmembrane
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
A0071870biological_processcellular response to catecholamine stimulus
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
A0120162biological_processpositive regulation of cold-induced thermogenesis
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007265biological_processRas protein signal transduction
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0070062cellular_componentextracellular exosome
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
B1903561cellular_componentextracellular vesicle
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
G0048144biological_processfibroblast proliferation
G0070062cellular_componentextracellular exosome
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI
ChainResidueDetails
RALA119-ILE135

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 Residues70
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
RMET-6-GLN27
RTHR96-CYS106
RARG175-ASN196
RGLN299-LYS305
ACYS237
ASER306
AARG380

site_idSWS_FT_FI2
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
RGLY35-ILE58

site_idSWS_FT_FI3
Number of Residues168
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
RALA59-PHE71
RASP130-ALA150
RARG221-THR274
RPRO323-ASN406

site_idSWS_FT_FI4
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
RILE72-LEU95

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
RGLU107-VAL129

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
RARG151-TYR174

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
RGLN197-SER220

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
RLEU275-ILE298

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
RGLU306-SER329

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
RASP113
RTHR118
RASN293
RASN312
RTYR316

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
RSER203

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
RTYR141

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332
ChainResidueDetails
RSER246

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
RSER261
RSER262

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails
RSER345
RSER346

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine; by BARK => ECO:0000305
ChainResidueDetails
RSER355
RSER356

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:19584355
ChainResidueDetails
RPRO390
RPRO403

site_idSWS_FT_FI18
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
RCYS265

site_idSWS_FT_FI19
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails
RCYS341

site_idSWS_FT_FI20
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
RASN-1
RASN8

219515

PDB entries from 2024-05-08

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