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9LYD

Cryo-EM structure of GPR3-1IU9 complex

Functional Information from GO Data
ChainGOidnamespacecontents
Q0003376biological_processsphingosine-1-phosphate receptor signaling pathway
Q0004930molecular_functionG protein-coupled receptor activity
Q0005515molecular_functionprotein binding
Q0005737cellular_componentcytoplasm
Q0005886cellular_componentplasma membrane
Q0007165biological_processsignal transduction
Q0007186biological_processG protein-coupled receptor signaling pathway
Q0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
Q0016020cellular_componentmembrane
Q0038036molecular_functionsphingosine-1-phosphate receptor activity
Q0040020biological_processregulation of meiotic nuclear division
Q0120162biological_processpositive regulation of cold-induced thermogenesis
R0003376biological_processsphingosine-1-phosphate receptor signaling pathway
R0004930molecular_functionG protein-coupled receptor activity
R0005515molecular_functionprotein binding
R0005737cellular_componentcytoplasm
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0038036molecular_functionsphingosine-1-phosphate receptor activity
R0040020biological_processregulation of meiotic nuclear division
R0120162biological_processpositive regulation of cold-induced thermogenesis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIgSLLAITVDRYLsL
ChainResidueDetails
QALA122-LEU138

site_idPS00924
Number of Residues11
DetailsASP_GLU_RACEMASE_2 Aspartate and glutamate racemases signature 2. IIaGCTEVSvV
ChainResidueDetails
QILE1088-VAL1098

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17847084","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17847084","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2DX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues62
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues78
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues38
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues36
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues52
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 335
ChainResidueDetails

site_idMCSA2
Number of Residues3
DetailsM-CSA 335
ChainResidueDetails

239492

PDB entries from 2025-07-30

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