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9OPY

Structure of the sweet receptor in the apo state

Functional Information from GO Data
ChainGOidnamespacecontents
A0001582biological_processdetection of chemical stimulus involved in sensory perception of sweet taste
A0004930molecular_functionG protein-coupled receptor activity
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0008527molecular_functiontaste receptor activity
A0016020cellular_componentmembrane
A0032467biological_processpositive regulation of cytokinesis
A0033041molecular_functionsweet taste receptor activity
A0043235cellular_componentreceptor complex
A0050909biological_processsensory perception of taste
A0050916biological_processsensory perception of sweet taste
A1903767cellular_componentsweet taste receptor complex
B0001582biological_processdetection of chemical stimulus involved in sensory perception of sweet taste
B0004888molecular_functiontransmembrane signaling receptor activity
B0004930molecular_functionG protein-coupled receptor activity
B0005515molecular_functionprotein binding
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0008527molecular_functiontaste receptor activity
B0033041molecular_functionsweet taste receptor activity
B0050909biological_processsensory perception of taste
B0050916biological_processsensory perception of sweet taste
B0050917biological_processsensory perception of umami taste
B1903767cellular_componentsweet taste receptor complex
Functional Information from PROSITE/UniProt
site_idPS00980
Number of Residues25
DetailsG_PROTEIN_RECEP_F3_2 G-protein coupled receptors family 3 signature 2. CCYdCvdCkagsYrkhp.DdfTCtpC
ChainResidueDetails
BCYS522-CYS546
ACYS513-CYS538

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues96
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues82
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues17
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; when associated with variant T-60","evidences":[{"source":"PubMed","id":"11326277","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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