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8XQR

Structure 2 of human class T GPCR TAS2R14-miniGs/gust complex with Flufenamic acid.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
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
C0005515molecular_functionprotein binding
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
C0016020cellular_componentmembrane
C0031681molecular_functionG-protein beta-subunit binding
C0045202cellular_componentsynapse
C0048144biological_processfibroblast proliferation
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
R0001580biological_processdetection of chemical stimulus involved in sensory perception of bitter taste
R0004930molecular_functionG protein-coupled receptor activity
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0008527molecular_functiontaste receptor activity
R0016020cellular_componentmembrane
R0033038molecular_functionbitter taste receptor activity
R0050909biological_processsensory perception of taste
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
BVAL327-GLY341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04896
ChainResidueDetails
AGLY43
ASER50
ALYS193
APHE200
ATHR219

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AARG197
RLEU109-VAL129
RTRP206-SER232
RGLY283-SER317

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
RILE56-PHE76

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
RALA77-ASN87
RHIS151-THR184
RSER254-LEU261

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:38600377, ECO:0000269|PubMed:38776963, ECO:0007744|PDB:8VY7, ECO:0007744|PDB:8VY9, ECO:0007744|PDB:8XQL, ECO:0007744|PDB:8XQN, ECO:0007744|PDB:8XQO, ECO:0007744|PDB:8XQP, ECO:0007744|PDB:8XQR, ECO:0007744|PDB:8XQS, ECO:0007744|PDB:8XQT, ECO:0007744|PDB:8YKY
ChainResidueDetails
RILE88-PHE108

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:38600377, ECO:0000269|PubMed:38776963, ECO:0007744|PDB:8VY7, ECO:0007744|PDB:8VY9, ECO:0007744|PDB:8XQL, ECO:0007744|PDB:8XQN, ECO:0007744|PDB:8XQO, ECO:0007744|PDB:8XQP, ECO:0007744|PDB:8XQR, ECO:0007744|PDB:8XQS, ECO:0007744|PDB:8XQT, ECO:0007744|PDB:8YKY
ChainResidueDetails
RVAL130-ILE150

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:38600377, ECO:0000269|PubMed:38776963, ECO:0007744|PDB:8VY7, ECO:0007744|PDB:8VY9, ECO:0007744|PDB:8XQL, ECO:0007744|PDB:8XQN, ECO:0007744|PDB:8XQO, ECO:0007744|PDB:8XQP, ECO:0007744|PDB:8XQR, ECO:0007744|PDB:8XQS, ECO:0007744|PDB:8XQT, ECO:0007744|PDB:8YKY
ChainResidueDetails
RVAL185-MET205

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:38600377, ECO:0000269|PubMed:38776963, ECO:0007744|PDB:8VY7, ECO:0007744|PDB:8VY9, ECO:0007744|PDB:8XQL, ECO:0007744|PDB:8XQN, ECO:0007744|PDB:8XQO, ECO:0007744|PDB:8XQP, ECO:0007744|PDB:8XQR, ECO:0007744|PDB:8XQS, ECO:0007744|PDB:8XQT, ECO:0007744|PDB:8YKY
ChainResidueDetails
RVAL233-THR253

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:38600377, ECO:0000269|PubMed:38776963, ECO:0007744|PDB:8VY7, ECO:0007744|PDB:8VY9, ECO:0007744|PDB:8XQL, ECO:0007744|PDB:8XQN, ECO:0007744|PDB:8XQO, ECO:0007744|PDB:8XQP, ECO:0007744|PDB:8XQR, ECO:0007744|PDB:8XQS, ECO:0007744|PDB:8XQT, ECO:0007744|PDB:8YKY
ChainResidueDetails
RILE262-LEU282

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:38600377, ECO:0000269|PubMed:38776963, ECO:0007744|PDB:8VY7, ECO:0007744|PDB:8VY9, ECO:0007744|PDB:8XQL, ECO:0007744|PDB:8XQN, ECO:0007744|PDB:8XQO, ECO:0007744|PDB:8XQP, ECO:0007744|PDB:8XQR, ECO:0007744|PDB:8XQS, ECO:0007744|PDB:8XQT, ECO:0007744|PDB:8YKY
ChainResidueDetails
RTHR86
RTRP89
RVAL180
RSER265
RMET268

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
RASN153

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN162
RASN171

235183

PDB entries from 2025-04-23

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