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8JLP

Ralmitaront(RO-6889450)-bound hTAAR1-Gs protein complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
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
R0001594molecular_functiontrace-amine receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0005506molecular_functioniron ion binding
R0005783cellular_componentendoplasmic reticulum
R0005789cellular_componentendoplasmic reticulum membrane
R0005886cellular_componentplasma membrane
R0007186biological_processG protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0008227molecular_functionG protein-coupled amine receptor activity
R0009055molecular_functionelectron transfer activity
R0012505cellular_componentendomembrane system
R0016020cellular_componentmembrane
R0020037molecular_functionheme binding
R0022900biological_processelectron transport chain
R0042597cellular_componentperiplasmic space
R0046872molecular_functionmetal ion binding
Y0005515molecular_functionprotein binding
Y0005834cellular_componentheterotrimeric G-protein complex
Y0005886cellular_componentplasma membrane
Y0007165biological_processsignal transduction
Y0007186biological_processG protein-coupled receptor signaling pathway
Y0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
Y0016020cellular_componentmembrane
Y0031681molecular_functionG-protein beta-subunit binding
Y0045202cellular_componentsynapse
Y0048144biological_processfibroblast proliferation
Y0070062cellular_componentextracellular exosome
Y0071380biological_processcellular response to prostaglandin E stimulus
Y0071870biological_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. ASIfHLSFISIDRYYaV
ChainResidueDetails
RALA109-VAL125

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:0000250|UniProtKB:P04896
ChainResidueDetails
AGLY47
AASN54
AASP223
AASN292
ASER366

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER352
RVAL82-CYS96
RGLU162-LYS188
RASP274-ASN286

site_idSWS_FT_FI3
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
ALYS300

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ASER174
RASP120-VAL139
RARG212-ALA249
RTYR308-SER339

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ALEU198

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0
ChainResidueDetails
ATHR204

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AARG201

site_idSWS_FT_FI8
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805
ChainResidueDetails
AGLY9

site_idSWS_FT_FI9
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
ACYS10

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37935377, ECO:0000269|PubMed:37963465
ChainResidueDetails
RASP287-PHE307

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37935377, ECO:0000269|PubMed:37963465, ECO:0007744|PDB:8W89, ECO:0007744|PDB:8WCA
ChainResidueDetails
RASP103

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN10
RASN17

226707

PDB entries from 2024-10-30

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