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8KEX

CryoEM structure of Gq coupled MRGPRX4 with agonist DCA-3P, local

Functional Information from GO Data
ChainGOidnamespacecontents
E0004888molecular_functiontransmembrane signaling receptor activity
E0004930molecular_functionG protein-coupled receptor activity
E0005506molecular_functioniron ion binding
E0005515molecular_functionprotein binding
E0005886cellular_componentplasma membrane
E0006091biological_processgeneration of precursor metabolites and energy
E0007186biological_processG protein-coupled receptor signaling pathway
E0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
E0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
E0008218biological_processbioluminescence
E0009055molecular_functionelectron transfer activity
E0016020cellular_componentmembrane
E0020037molecular_functionheme binding
E0022900biological_processelectron transport chain
E0038182molecular_functionG protein-coupled bile acid receptor activity
E0038184biological_processadenylate cyclase-activating G protein-coupled bile acid receptor signaling pathway
E0042597cellular_componentperiplasmic space
E0160025biological_processsensory perception of itch
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TGLsMLSAISTERCLsV
ChainResidueDetails
ETHR108-VAL124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues15
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"34789874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7S8P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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