5WIU
Structure of the human D4 Dopamine receptor in complex with Nemonapride
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004952 | molecular_function | dopamine neurotransmitter 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 | 0007195 | biological_process | adenylate cyclase-inhibiting dopamine 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue AQD A 1201 |
| Chain | Residue |
| A | LEU111 |
| A | THR434 |
| A | TYR438 |
| A | HOH1326 |
| A | ASP115 |
| A | THR120 |
| A | LEU187 |
| A | VAL193 |
| A | SER196 |
| A | SER200 |
| A | PHE410 |
| A | PHE411 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 1202 |
| Chain | Residue |
| A | TYR143 |
| A | GLY148 |
| A | SER149 |
| A | ARG151 |
| A | GLN152 |
| A | GOL1223 |
| A | HOH1352 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue PO4 A 1203 |
| Chain | Residue |
| A | ARG390 |
| A | ARG390 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 1204 |
| Chain | Residue |
| A | LEU85 |
| A | LEU85 |
| A | HOH1379 |
| A | HOH1379 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue OLA A 1205 |
| Chain | Residue |
| A | VAL59 |
| A | THR67 |
| A | ASN70 |
| A | SER71 |
| A | SER75 |
| A | LEU153 |
| A | TRP160 |
| A | PEG1221 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1206 |
| Chain | Residue |
| A | LEU44 |
| A | ALA47 |
| A | GLU95 |
| A | TRP435 |
| A | OLA1207 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1207 |
| Chain | Residue |
| A | ARG428 |
| A | SER431 |
| A | ALA432 |
| A | OLA1206 |
| A | HOH1316 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue OLA A 1208 |
| Chain | Residue |
| A | PHE124 |
| A | ASP132 |
| A | ARG151 |
| A | LEU155 |
| A | LEU162 |
| A | TYR195 |
| A | HOH1367 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 1209 |
| Chain | Residue |
| A | LEU54 |
| A | SER58 |
| A | PRO445 |
| A | THR449 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 1210 |
| Chain | Residue |
| A | LEU209 |
| A | PHE216 |
| A | GLN220 |
| A | ARG390 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1211 |
| Chain | Residue |
| A | PHE134 |
| A | ALA138 |
| A | ASP191 |
| A | CYS199 |
| A | HOH1365 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1212 |
| Chain | Residue |
| A | GLY401 |
| A | ALA402 |
| A | PHE451 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 1213 |
| Chain | Residue |
| A | PHE202 |
| A | THR416 |
| A | ARG428 |
| A | GLU1081 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1214 |
| Chain | Residue |
| A | LEU429 |
| A | HOH1301 |
| A | HOH1301 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 1216 |
| Chain | Residue |
| A | MET114 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 1218 |
| Chain | Residue |
| A | SER53 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1219 |
| Chain | Residue |
| A | TYR93 |
| A | LEU103 |
| A | SER104 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1220 |
| Chain | Residue |
| A | SER104 |
| A | ARG106 |
| A | HOH1369 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 1221 |
| Chain | Residue |
| A | OLA1205 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 1223 |
| Chain | Residue |
| A | ARG133 |
| A | ALA136 |
| A | ARG151 |
| A | PO41202 |
| A | HOH1367 |
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. ASIfNLCAISVDRFVaV |
| Chain | Residue | Details |
| A | ALA121-VAL137 |
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 | 40 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29051383","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29051383","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 31 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29051383","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29051383","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":"29051383","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29051383","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":"29051383","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29051383","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 15 |
| Details | Repeat: {"description":"1; approximate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 15 |
| Details | Repeat: {"description":"2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 34 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 16 |
| Details | Compositional bias: {"description":"Pro residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29051383","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29051383","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5WIU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5WIV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
