7WC7
Crystal structure of serotonin 2A receptor in complex with lisuride
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 | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 13 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 31 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"36171289","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RAN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Motif: {"description":"DRY motif; important for ligand-induced conformation changes","evidences":[{"source":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]} |
| 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":"UniProtKB","id":"P41595","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"35084960","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WC4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"35084960","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7WC4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| 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_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24637012","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
