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7SRR

5-HT2B receptor bound to LSD in complex with heterotrimeric mini-Gq protein obtained by cryo-electron microscopy (cryoEM)

Functional Information from GO Data
ChainGOidnamespacecontents
B0003924molecular_functionGTPase activity
B0005525molecular_functionGTP binding
B0007186biological_processG protein-coupled receptor signaling pathway
B0019001molecular_functionguanyl nucleotide binding
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
C0001750cellular_componentphotoreceptor outer segment
C0003924molecular_functionGTPase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005829cellular_componentcytosol
C0005834cellular_componentheterotrimeric G-protein complex
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0007186biological_processG protein-coupled receptor signaling pathway
C0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
C0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
C0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
C0007265biological_processRas protein signal transduction
C0008283biological_processcell population proliferation
C0016020cellular_componentmembrane
C0030159molecular_functionsignaling receptor complex adaptor activity
C0044877molecular_functionprotein-containing complex binding
C0045202cellular_componentsynapse
C0050909biological_processsensory perception of taste
C0051020molecular_functionGTPase binding
C0060041biological_processretina development in camera-type eye
C0070062cellular_componentextracellular exosome
C0071380biological_processcellular response to prostaglandin E stimulus
C0071870biological_processcellular response to catecholamine stimulus
C0097381cellular_componentphotoreceptor disc membrane
C1903561cellular_componentextracellular vesicle
D0005515molecular_functionprotein binding
D0005834cellular_componentheterotrimeric G-protein complex
D0005886cellular_componentplasma membrane
D0007165biological_processsignal transduction
D0007186biological_processG protein-coupled receptor signaling pathway
D0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
D0016020cellular_componentmembrane
D0031681molecular_functionG-protein beta-subunit binding
D0048144biological_processfibroblast proliferation
D0070062cellular_componentextracellular exosome
D0071380biological_processcellular response to prostaglandin E stimulus
D0071870biological_processcellular response to catecholamine stimulus
R0004930molecular_functionG protein-coupled receptor activity
R0004993molecular_functionG protein-coupled serotonin receptor activity
R0005886cellular_componentplasma membrane
R0006939biological_processsmooth muscle contraction
R0007186biological_processG protein-coupled receptor signaling pathway
R0007507biological_processheart development
R0016020cellular_componentmembrane
R0042310biological_processvasoconstriction
R0050795biological_processregulation of behavior
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwHLCAISVDRYIaI
ChainResidueDetails
RALA141-ILE157

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
CLEU70-SER84
CILE157-ILE171
CLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RALA57-VAL79

site_idSWS_FT_FI2
Number of Residues113
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RSER80-ASN90
RASP152-THR171
RTHR240-LYS324

site_idSWS_FT_FI3
Number of Residues22
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RTYR91-LEU113

site_idSWS_FT_FI4
Number of Residues52
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RTHR114-PRO129
RLYS193-ASP216
RTHR346-MET360

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RALA130-VAL151

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RALA172-ILE192

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RPHE217-LEU239

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RVAL325-ILE345

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538
ChainResidueDetails
RLEU361-LEU382

site_idSWS_FT_FI10
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23519215, ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3
ChainResidueDetails
RASP135
RTHR140
RLEU209

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538
ChainResidueDetails
RLEU209

site_idSWS_FT_FI12
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
RCYS397

222926

PDB entries from 2024-07-24

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