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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8Z9O

Cryo-EM structure of human GPR4-Gs complex

Functional Information from GO Data
ChainGOidnamespacecontents
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
C0000166molecular_functionnucleotide binding
C0001678biological_processintracellular glucose homeostasis
C0002862biological_processnegative regulation of inflammatory response to antigenic stimulus
C0003091biological_processrenal water homeostasis
C0003924molecular_functionGTPase activity
C0003925molecular_functionG protein activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
C0007190biological_processactivation of adenylate cyclase activity
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0007192biological_processadenylate cyclase-activating serotonin receptor signaling pathway
C0007608biological_processsensory perception of smell
C0010856molecular_functionadenylate cyclase activator activity
C0014819biological_processregulation of skeletal muscle contraction
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0031748molecular_functionD1 dopamine receptor binding
C0032024biological_processpositive regulation of insulin secretion
C0032588cellular_componenttrans-Golgi network membrane
C0034695biological_processresponse to prostaglandin E
C0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
C0038184biological_processadenylate cyclase-activating G protein-coupled bile acid receptor signaling pathway
C0046872molecular_functionmetal ion binding
C0046907biological_processintracellular transport
C0048589biological_processdevelopmental growth
C0050890biological_processcognition
C0060348biological_processbone development
C0060789biological_processhair follicle placode formation
C0070062cellular_componentextracellular exosome
C0070527biological_processplatelet aggregation
C0071377biological_processcellular response to glucagon stimulus
C0071380biological_processcellular response to prostaglandin E stimulus
C0071468biological_processcellular response to acidic pH
C0071870biological_processcellular response to catecholamine stimulus
C0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
C0097700biological_processvascular endothelial cell response to laminar fluid shear stress
C0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ISIaFLCCISVDRYLaV
ChainResidueDetails
RILE103-VAL119
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 Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues30
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"UniProtKB","id":"P62871","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04896","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues36
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues13
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues30
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues28
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues35
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues37
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues35
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"9BIP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues15
DetailsRegion: {"description":"Extracellular loop 2 (ECL2)","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsSite: {"description":"Required for activation","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsSite: {"description":"Proton sensing","evidences":[{"source":"PubMed","id":"39753132","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsSite: {"description":"Proton sensing","evidences":[{"source":"UniProtKB","id":"Q8BUD0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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