9F33
Cryo-EM structure of Dopamine 3 Receptor:Go complex bound to bitopic FOB02-04A - Conformation A
This is a non-PDB format compatible entry.
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. ASIwNLCAISIDRYTaV |
Chain | Residue | Details |
R | ALA116-VAL132 |
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS |
Chain | Residue | Details |
B | LEU70-SER84 | |
B | ILE157-ILE171 | |
B | LEU285-ALA299 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132 |
Chain | Residue | Details |
R | TYR-179 | |
A | THR182 | |
A | ASN270 | |
A | ASP273 | |
A | CYS325 | |
A | LYS46 | |
A | ASN47 | |
A | THR48 | |
A | SER152 | |
A | LEU176 | |
A | ARG177 | |
A | THR178 | |
A | ARG179 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132 |
Chain | Residue | Details |
R | THR-180 | |
R | GLY-178 |
site_id | SWS_FT_FI3 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | ALA33-LEU55 |
site_id | SWS_FT_FI4 |
Number of Residues | 163 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | LYS56-ASN65 | |
R | ASP127-ARG149 | |
R | ARG210-GLN329 | |
R | ASN387-CYS400 |
site_id | SWS_FT_FI5 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | TYR66-TYR88 |
site_id | SWS_FT_FI6 |
Number of Residues | 45 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | LEU89-ASP104 | |
R | GLY171-ASP187 | |
R | ASN352-SER366 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | VAL105-ILE126 |
site_id | SWS_FT_FI8 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | VAL150-PHE170 |
site_id | SWS_FT_FI9 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | PHE188-ALA209 |
site_id | SWS_FT_FI10 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | MET330-LEU351 |
site_id | SWS_FT_FI11 |
Number of Residues | 19 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:21097933 |
Chain | Residue | Details |
R | ALA367-PHE386 |
site_id | SWS_FT_FI12 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21097933, ECO:0007744|PDB:3PBL |
Chain | Residue | Details |
R | ASP110 | |
R | PHE345 | |
R | HIS349 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
R | ASN12 | |
R | ASN19 | |
R | ASN97 | |
R | ASN173 |