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 | 44 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | LEU35-ALA57 | |
B | LEU35-ALA57 |
site_id | SWS_FT_FI2 |
Number of Residues | 86 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | SER58-ASN67 | |
A | ASP129-CYS146 | |
A | ILE370-CYS387 | |
B | SER58-ASN67 | |
B | ASP129-CYS146 | |
B | ILE370-CYS387 |
site_id | SWS_FT_FI3 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | TYR68-TYR90 | |
B | TYR68-TYR90 |
site_id | SWS_FT_FI4 |
Number of Residues | 76 |
Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | SER91-ASP106 | |
A | ASP171-ASP186 | |
A | ALA338-SER346 | |
B | SER91-ASP106 | |
B | ASP171-ASP186 | |
B | ALA338-SER346 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | THR107-VAL128 | |
B | THR107-VAL128 |
site_id | SWS_FT_FI6 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | GLN147-ASN170 | |
B | GLN147-ASN170 |
site_id | SWS_FT_FI7 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | TYR187-TRP208 | |
B | TYR187-TRP208 |
site_id | SWS_FT_FI8 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | VAL315-ARG337 | |
B | VAL315-ARG337 |
site_id | SWS_FT_FI9 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | PRO347-THR369 | |
B | PRO347-THR369 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | ASP77 | |
A | SER119 | |
B | ASP77 | |
B | SER119 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P21917 |
Chain | Residue | Details |
A | CYS387 | |
B | CYS387 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP1007 | |
A | ILE1102 | |
B | TRP1007 | |
B | ILE1102 |