6A93
Crystal structure of 5-HT2AR in complex with risperidone
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue 8NU A 3001 |
| Chain | Residue |
| A | SER131 |
| A | PHE332 |
| A | TRP336 |
| A | PHE339 |
| A | PHE340 |
| A | LEU362 |
| A | ASN363 |
| A | TYR370 |
| A | TRP151 |
| A | ASP155 |
| A | SER159 |
| A | THR160 |
| A | ILE163 |
| A | LEU228 |
| A | SER242 |
| A | PHE243 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CLR A 3002 |
| Chain | Residue |
| A | MET114 |
| A | ILE118 |
| A | TYR153 |
| A | PHE193 |
| A | ILE196 |
| A | TRP200 |
| A | VAL204 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 3003 |
| Chain | Residue |
| A | HIS182 |
| A | HIS183 |
| A | GLU264 |
| A | GLU318 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue 1PE A 3004 |
| Chain | Residue |
| A | SER226 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue 1PE A 3005 |
| Chain | Residue |
| A | LEU261 |
| A | GLN262 |
| A | ALA265 |
| A | ILE315 |
| A | GLN319 |
| A | GLU1004 |
| A | ASN1080 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue 1PE A 3006 |
| Chain | Residue |
| A | GLU1004 |
| A | TRP1007 |
| A | LYS1027 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | binding site for residue 8NU B 3001 |
| Chain | Residue |
| B | SER131 |
| B | TRP151 |
| B | ASP155 |
| B | VAL156 |
| B | SER159 |
| B | THR160 |
| B | ILE163 |
| B | LEU228 |
| B | SER242 |
| B | PHE332 |
| B | TRP336 |
| B | PHE339 |
| B | PHE340 |
| B | ASN363 |
| B | TYR370 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue PLM B 3002 |
| Chain | Residue |
| B | ILE395 |
| B | GLN396 |
| B | CYS397 |
| B | CLR3003 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CLR B 3003 |
| Chain | Residue |
| B | LEU94 |
| B | TYR394 |
| B | TYR399 |
| B | PLM3002 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| 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 | 45 |
| 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 | 50 |
| 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 | 62 |
| 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 | 48 |
| 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 | 50 |
| 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 | 50 |
| 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 | 50 |
| 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 | 4 |
| 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 | 8 |
| 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 | 2 |
| 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 | 2 |
| 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 | 2 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24637012","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
