Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7VDM

Cryo-EM structure of pseudoallergen receptor MRGPRX2 complex with substance P

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005813cellular_componentcentrosome
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0019001molecular_functionguanyl nucleotide binding
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031749molecular_functionD2 dopamine receptor binding
A0031821molecular_functionG protein-coupled serotonin receptor binding
A0043434biological_processresponse to peptide hormone
A0043949biological_processregulation of cAMP-mediated signaling
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A0072678biological_processT cell migration
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
B0007265biological_processRas protein signal transduction
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0070062cellular_componentextracellular exosome
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
B1903561cellular_componentextracellular vesicle
G0005834cellular_componentheterotrimeric G-protein complex
G0007186biological_processG protein-coupled receptor signaling pathway
G0031681molecular_functionG-protein beta-subunit binding
L0007217biological_processtachykinin receptor signaling pathway
R0004930molecular_functionG protein-coupled receptor activity
R0005886cellular_componentplasma membrane
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
R0019233biological_processsensory perception of pain
R0030431biological_processsleep
R0032467biological_processpositive regulation of cytokinesis
R0042923molecular_functionneuropeptide binding
R0043303biological_processmast cell degranulation
R0045576biological_processmast cell activation
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

site_idPS00267
Number of Residues5
DetailsTACHYKININ Tachykinin family signature. FFGLM
ChainResidueDetails
LPHE7-MET11

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by FAP => ECO:0000269|PubMed:21314817
ChainResidueDetails
LPRO2
RASN85-SER96
RLYS166-ASP184
RTRP250-SER264

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by MME => ECO:0000269|PubMed:6208535
ChainResidueDetails
LGLN6
LPHE7

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Cleavage; by ACE => ECO:0000269|PubMed:6208535
ChainResidueDetails
LPHE8
RSER118-HIS144
RLEU206-THR228
RARG286-VAL330

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage; by ACE and MME => ECO:0000269|PubMed:6208535
ChainResidueDetails
LGLY9

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Methionine amide => ECO:0000269|PubMed:3770210
ChainResidueDetails
LMET11

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
RLEU145-GLY165

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
RPHE185-LEU205

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RVAL229-ILE249

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RVAL265-PHE285

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805
ChainResidueDetails
AGLY2

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
ACYS3

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon