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9M1H

Cryo-EM structure of PGE2-EP1-Gq complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0004957molecular_functionprostaglandin E receptor activity
A0005886cellular_componentplasma membrane
A0006954biological_processinflammatory response
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
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0007204biological_processpositive regulation of cytosolic calcium ion concentration
A0007206biological_processphospholipase C-activating G protein-coupled glutamate receptor signaling pathway
A0016020cellular_componentmembrane
A0031748molecular_functionD1 dopamine receptor binding
A0032496biological_processresponse to lipopolysaccharide
A0034695biological_processresponse to prostaglandin E
C0001750cellular_componentphotoreceptor outer segment
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005829cellular_componentcytosol
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
C0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
C0007265biological_processRas protein signal transduction
C0008283biological_processcell population proliferation
C0016020cellular_componentmembrane
C0030159molecular_functionsignaling receptor complex adaptor activity
C0044877molecular_functionprotein-containing complex binding
C0045202cellular_componentsynapse
C0050909biological_processsensory perception of taste
C0051020molecular_functionGTPase binding
C0060041biological_processretina development in camera-type eye
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
C0097381cellular_componentphotoreceptor disc membrane
C1903561cellular_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
G0045202cellular_componentsynapse
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. CPLlLGCGMAVERCVgV
ChainResidueDetails
ACYS123-VAL139

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
CLEU75-SER89
CILE162-ILE176
CLEU290-ALA304

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378
ChainResidueDetails
GALA1
AARG97-HIS111
AARG178-ALA201
AGLY322-PRO332

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
GCYS67

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
GCYS67
BGLY40
BSER47
BASP200
BASN259
BSER333

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
BARG178

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805
ChainResidueDetails
BGLY2

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
BCYS3

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER319

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
BLYS267

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
ALEU333-LEU354

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN8
AASN25

237735

PDB entries from 2025-06-18

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