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7SRQ

5-HT2B receptor bound to LSD obtained by cryo-electron microscopy (cryoEM)

Functional Information from GO Data
ChainGOidnamespacecontents
R0004930molecular_functionG protein-coupled receptor activity
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
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

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, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
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, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
ChainResidueDetails
RSER80-ASN90
RASP152-THR171
RTHR240-PHE383

site_idSWS_FT_FI3
Number of Residues22
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
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, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
ChainResidueDetails
RTHR114-PRO129
RLYS193-ASP216

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
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, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
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, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
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, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
ChainResidueDetails
RASN384-SER404

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538, ECO:0000269|PubMed:30127358, ECO:0000269|PubMed:36087581
ChainResidueDetails

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

227111

PDB entries from 2024-11-06

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