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7Y26

Cryo-EM structure of the octreotide-bound SSTR2-miniGq-scFv16 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0001750cellular_componentphotoreceptor outer segment
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005829cellular_componentcytosol
A0005834cellular_componentheterotrimeric G-protein complex
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
A0007265biological_processRas protein signal transduction
A0008283biological_processcell population proliferation
A0016020cellular_componentmembrane
A0030159molecular_functionsignaling receptor complex adaptor activity
A0044877molecular_functionprotein-containing complex binding
A0045202cellular_componentsynapse
A0050909biological_processsensory perception of taste
A0051020molecular_functionGTPase binding
A0060041biological_processretina development in camera-type eye
A0070062cellular_componentextracellular exosome
A0071380biological_processcellular response to prostaglandin E stimulus
A0071870biological_processcellular response to catecholamine stimulus
A0097381cellular_componentphotoreceptor disc membrane
A1903561cellular_componentextracellular vesicle
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007186biological_processG protein-coupled receptor signaling pathway
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
E0004930molecular_functionG protein-coupled receptor activity
E0004994molecular_functionsomatostatin receptor activity
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0007186biological_processG protein-coupled receptor signaling pathway
E0007187biological_processG protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger
E0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
E0007218biological_processneuropeptide signaling pathway
E0007283biological_processspermatogenesis
E0008285biological_processnegative regulation of cell population proliferation
E0016020cellular_componentmembrane
E0021549biological_processcerebellum development
E0030165molecular_functionPDZ domain binding
E0030432biological_processperistalsis
E0030900biological_processforebrain development
E0038170biological_processsomatostatin signaling pathway
E0042594biological_processresponse to starvation
E0042923molecular_functionneuropeptide binding
E0043005cellular_componentneuron projection
E0071385biological_processcellular response to glucocorticoid stimulus
E0071392biological_processcellular response to estradiol stimulus
F0005515molecular_functionprotein binding
F0005834cellular_componentheterotrimeric G-protein complex
F0005886cellular_componentplasma membrane
F0007165biological_processsignal transduction
F0007186biological_processG protein-coupled receptor signaling pathway
F0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
F0016020cellular_componentmembrane
F0031681molecular_functionG-protein beta-subunit binding
F0048144biological_processfibroblast proliferation
F0070062cellular_componentextracellular exosome
F0071380biological_processcellular response to prostaglandin E stimulus
F0071870biological_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. TSIfCLTVMSIDRYLaV
ChainResidueDetails
ETHR128-VAL144

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
ALEU70-SER84
AILE157-ILE171
ALEU285-ALA299

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
FALA2
EALA104-VAL118
EGLY182-GLY207
ESER279-PRO288

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine methyl ester => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
FSER68

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: S-geranylgeranyl cysteine => ECO:0000250|UniProtKB:P63212
ChainResidueDetails
FSER68
EASP139-MET161
EPHE230-LYS253

site_idSWS_FT_FI4
Number of Residues24
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
EASN79-VAL103

site_idSWS_FT_FI5
Number of Residues19
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
EMET119-ILE138

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
EILE162-ALA181

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
EPHE208-LEU229

site_idSWS_FT_FI8
Number of Residues24
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
EVAL254-SER278

site_idSWS_FT_FI9
Number of Residues14
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
EALA289-ALA303

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Important for ligand binding
ChainResidueDetails
EASP89

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
ECYS328

site_idSWS_FT_FI12
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
EASN9
EASN22
EASN29
EASN32

221371

PDB entries from 2024-06-19

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