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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9L8L

Structure of GPCR megacomplex bound to agonists

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
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
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
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
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
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
C0000139cellular_componentGolgi membrane
C0000785cellular_componentchromatin
C0001664molecular_functionG protein-coupled receptor binding
C0001678biological_processintracellular glucose homeostasis
C0001934biological_processpositive regulation of protein phosphorylation
C0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
C0002031biological_processG protein-coupled receptor internalization
C0002092biological_processpositive regulation of receptor internalization
C0003713molecular_functiontranscription coactivator activity
C0004402molecular_functionhistone acetyltransferase activity
C0004857molecular_functionenzyme inhibitor activity
C0004869molecular_functioncysteine-type endopeptidase inhibitor activity
C0005096molecular_functionGTPase activator activity
C0005159molecular_functioninsulin-like growth factor receptor binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005905cellular_componentclathrin-coated pit
C0005929cellular_componentcilium
C0006357biological_processregulation of transcription by RNA polymerase II
C0006511biological_processubiquitin-dependent protein catabolic process
C0007166biological_processcell surface receptor signaling pathway
C0007600biological_processsensory perception
C0016567biological_processprotein ubiquitination
C0019899molecular_functionenzyme binding
C0030659cellular_componentcytoplasmic vesicle membrane
C0030666cellular_componentendocytic vesicle membrane
C0030674molecular_functionprotein-macromolecule adaptor activity
C0031143cellular_componentpseudopodium
C0031397biological_processnegative regulation of protein ubiquitination
C0031410cellular_componentcytoplasmic vesicle
C0031434molecular_functionmitogen-activated protein kinase kinase binding
C0031625molecular_functionubiquitin protein ligase binding
C0031701molecular_functionangiotensin receptor binding
C0032715biological_processnegative regulation of interleukin-6 production
C0032717biological_processnegative regulation of interleukin-8 production
C0035025biological_processpositive regulation of Rho protein signal transduction
C0035721biological_processintraciliary retrograde transport
C0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
C0042981biological_processregulation of apoptotic process
C0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
C0043149biological_processstress fiber assembly
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0045746biological_processnegative regulation of Notch signaling pathway
C0045880biological_processpositive regulation of smoothened signaling pathway
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0060090molecular_functionmolecular adaptor activity
C0070374biological_processpositive regulation of ERK1 and ERK2 cascade
C0097499biological_processprotein localization to non-motile cilium
C1902533biological_processpositive regulation of intracellular signal transduction
C1903568biological_processnegative regulation of protein localization to ciliary membrane
C1990763molecular_functionarrestin family protein binding
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
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
R0001540molecular_functionamyloid-beta binding
R0002025biological_processnorepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure
R0004939molecular_functionbeta-adrenergic receptor activity
R0004941molecular_functionbeta2-adrenergic receptor activity
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0005764cellular_componentlysosome
R0005768cellular_componentendosome
R0005794cellular_componentGolgi apparatus
R0005886cellular_componentplasma membrane
R0006898biological_processreceptor-mediated endocytosis
R0007166biological_processcell surface receptor signaling pathway
R0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
R0008179molecular_functionadenylate cyclase binding
R0008333biological_processendosome to lysosome transport
R0010008cellular_componentendosome membrane
R0010666biological_processpositive regulation of cardiac muscle cell apoptotic process
R0010667biological_processnegative regulation of cardiac muscle cell apoptotic process
R0015459molecular_functionpotassium channel regulator activity
R0016020cellular_componentmembrane
R0016324cellular_componentapical plasma membrane
R0019899molecular_functionenzyme binding
R0030669cellular_componentclathrin-coated endocytic vesicle membrane
R0042802molecular_functionidentical protein binding
R0042803molecular_functionprotein homodimerization activity
R0043235cellular_componentsignaling receptor complex
R0043410biological_processpositive regulation of MAPK cascade
R0044877molecular_functionprotein-containing complex binding
R0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
R0051380molecular_functionnorepinephrine binding
R0061885biological_processpositive regulation of mini excitatory postsynaptic potential
R0071875biological_processadrenergic receptor signaling pathway
R0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
R0071881biological_processadenylate cyclase-inhibiting adrenergic receptor signaling pathway
R0098990biological_processAMPA selective glutamate receptor signaling pathway
R0098992cellular_componentneuronal dense core vesicle
R0106134biological_processpositive regulation of cardiac muscle cell contraction
R0120162biological_processpositive regulation of cold-induced thermogenesis
R1900451biological_processpositive regulation of glutamate receptor signaling pathway
R1901098biological_processpositive regulation of autophagosome maturation
R1904504biological_processpositive regulation of lipophagy
R1904646biological_processcellular response to amyloid-beta
R1990911biological_processresponse to psychosocial stress
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_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
CPHE61-LEU79
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 Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10427002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11087399","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15591060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19243146","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9395396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9417641","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16766715","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P63092","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues11
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D4S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17952055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8521811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2540197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

254587

PDB entries from 2026-06-03

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