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7VV4

Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with linear cortistatin-14, local

Functional Information from GO Data
ChainGOidnamespacecontents
L0005179molecular_functionhormone activity
L0005576cellular_componentextracellular region
R0001819biological_processpositive regulation of cytokine production
R0004930molecular_functionG protein-coupled receptor activity
R0004985molecular_functionG protein-coupled opioid receptor activity
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
R0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0016477biological_processcell migration
R0016493molecular_functionC-C chemokine receptor activity
R0019233biological_processsensory perception of pain
R0030431biological_processsleep
R0032467biological_processpositive regulation of cytokinesis
R0032722biological_processpositive regulation of chemokine production
R0038003biological_processG protein-coupled opioid receptor signaling pathway
R0042923molecular_functionneuropeptide binding
R0043303biological_processmast cell degranulation
R0045576biological_processmast cell activation
R0048265biological_processresponse to pain
R0070098biological_processchemokine-mediated signaling pathway
R1902624biological_processpositive regulation of neutrophil migration
R1990595molecular_functionmast cell secretagogue receptor activity
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. AGLsMLSTVSTERCLsV
ChainResidueDetails
RALA115-VAL131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues56
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues43
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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