6IQL
Crystal structure of dopamine receptor D4 bound to the subtype-selective ligand, L745870
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 |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004952 | molecular_function | dopamine neurotransmitter 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 | 0007195 | biological_process | adenylate cyclase-inhibiting dopamine 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue L74 A 1201 |
| Chain | Residue |
| A | PHE88 |
| A | TYR358 |
| A | SER91 |
| A | GLY96 |
| A | TRP98 |
| A | MET109 |
| A | ASP112 |
| A | VAL113 |
| A | PHE330 |
| A | PHE331 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue L74 B 1201 |
| Chain | Residue |
| B | PHE88 |
| B | SER91 |
| B | GLY96 |
| B | TRP98 |
| B | ASP112 |
| B | VAL113 |
| B | CYS180 |
| B | PHE330 |
| B | TYR358 |
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. ASIwNLCAISVDRFVaV |
| Chain | Residue | Details |
| A | ALA118-VAL134 |
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 | 44 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 46 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P21917","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
