6WH4
Crystal structure of HTR2A with inverse agonist
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 | 
| A | 0042597 | cellular_component | periplasmic space | 
| A | 0046872 | molecular_function | metal ion binding | 
| B | 0004930 | molecular_function | G protein-coupled receptor activity | 
| B | 0004993 | molecular_function | G protein-coupled serotonin receptor activity | 
| B | 0005506 | molecular_function | iron ion binding | 
| B | 0005886 | cellular_component | plasma membrane | 
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway | 
| B | 0009055 | molecular_function | electron transfer activity | 
| B | 0016020 | cellular_component | membrane | 
| B | 0020037 | molecular_function | heme binding | 
| B | 0022900 | biological_process | electron transport chain | 
| B | 0042597 | cellular_component | periplasmic space | 
| B | 0046872 | molecular_function | metal ion binding | 
| C | 0004930 | molecular_function | G protein-coupled receptor activity | 
| C | 0004993 | molecular_function | G protein-coupled serotonin receptor activity | 
| C | 0005506 | molecular_function | iron ion binding | 
| C | 0005886 | cellular_component | plasma membrane | 
| C | 0007186 | biological_process | G protein-coupled receptor signaling pathway | 
| C | 0009055 | molecular_function | electron transfer activity | 
| C | 0016020 | cellular_component | membrane | 
| C | 0020037 | molecular_function | heme binding | 
| C | 0022900 | biological_process | electron transport chain | 
| C | 0042597 | cellular_component | periplasmic space | 
| C | 0046872 | molecular_function | metal ion binding | 
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. ASImHLCAISLDRYVaI | 
| Chain | Residue | Details | 
| A | ALA161-ILE177 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 6 | 
| Details | Binding site: {"description":"axial binding residue"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 48 | 
| 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 | 58 | 
| 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 | 75 | 
| 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 | 61 | 
| 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 | 72 | 
| 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 | 46 | 
| 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 | 75 | 
| 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 | 75 | 
| 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 | 75 | 
| 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 | 6 | 
| 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 | 12 | 
| 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 | 3 | 
| 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 | 3 | 
| 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 | 3 | 
| 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 | 






