7SRS
5-HT2B receptor bound to LSD in complex with beta-arrestin1 obtained by cryo-electron microscopy (cryoEM)
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00237 |
Number of Residues | 17 |
Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwHLCAISVDRYIaI |
Chain | Residue | Details |
R | ALA141-ILE157 |
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH |
Chain | Residue | Details |
P | TYR191-HIS197 | |
Q | TYR201-HIS207 |
site_id | PS00295 |
Number of Residues | 19 |
Details | ARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL |
Chain | Residue | Details |
C | PHE61-LEU79 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 29 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 52 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 22 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 21 |
Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24357322","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30127358","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36087581","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Motif: {"description":"DRY motif; important for ligand-induced conformation changes","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 3 |
Details | Motif: {"description":"[DE]RFG motif; may stabilize a conformation that preferentially activates signaling via beta-arrestin family members","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | Motif: {"description":"NPxxY motif; important for ligand-induced conformation changes and signaling","evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23519215","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IB4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NC3","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | Site: {"description":"Hydrophobic barrier that decreases the speed of ligand binding and dissociation","evidences":[{"source":"PubMed","id":"28129538","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI16 |
Number of Residues | 41 |
Details | Region: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI17 |
Number of Residues | 11 |
Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI18 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |