7WC4
Crystal structure of serotonin 2A receptor in complex with serotonin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0004993 | molecular_function | G protein-coupled serotonin receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | THR81-MET97 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | ALA98-TYR111 | |
A | ASP172-LYS191 |
site_id | SWS_FT_FI3 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | PHE112-TYR137 |
site_id | SWS_FT_FI4 |
Number of Residues | 31 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | GLY138-LYS146 | |
A | GLN216-ASP232 | |
A | CYS349-ASP356 |
site_id | SWS_FT_FI5 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | LEU147-LEU171 |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | ALA192-LEU215 |
site_id | SWS_FT_FI7 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | ASN233-ILE258 |
site_id | SWS_FT_FI8 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | LYS323-ILE348 |
site_id | SWS_FT_FI9 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN |
Chain | Residue | Details |
A | VAL357-LEU382 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:35084960, ECO:0007744|PDB:7WC4 |
Chain | Residue | Details |
A | ASP155 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:35084960, ECO:0007744|PDB:7WC4 |
Chain | Residue | Details |
A | ASN343 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | SITE: Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538 |
Chain | Residue | Details |
A | LEU229 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:24637012 |
Chain | Residue | Details |
A | ALA1037 |