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8IYW

Structure of GSK256073-GPR109A-G-protein complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007186biological_processG protein-coupled receptor signaling pathway
B0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
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
G0048144biological_processfibroblast proliferation
G0070062cellular_componentextracellular exosome
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
R0001781biological_processneutrophil apoptotic process
R0004930molecular_functionG protein-coupled receptor activity
R0005886cellular_componentplasma membrane
R0006915biological_processapoptotic process
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0030054cellular_componentcell junction
R0033031biological_processpositive regulation of neutrophil apoptotic process
R0050995biological_processnegative regulation of lipid catabolic process
R0070165biological_processpositive regulation of adiponectin secretion
R0070553molecular_functionnicotinic acid receptor activity
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. GSIiFLTVVAVDRYFrV
ChainResidueDetails
RGLY113-VAL129

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
CLEU70-SER84
CILE157-ILE171
CLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN-24
RASN-19
BTHR182
BASP201
BLYS280
BPHE336

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
RLEU34-PHE54

site_idSWS_FT_FI3
Number of Residues109
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
RHIS55-ARG63
RASP124-ARG142
RSER214-ALA229
RTYR295-PRO363

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
RILE64-MET84

site_idSWS_FT_FI5
Number of Residues67
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
RASP85-LEU102
RLYS164-MET192
RARG251-ASP273

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
RMET103-VAL123

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RTHR143-LEU163

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RPHE193-TRP213

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RILE230-VAL250

site_idSWS_FT_FI10
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RLEU274-TYR294

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9EP66
ChainResidueDetails
RSER328

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PDB entries from 2024-07-24

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