3PBL
Structure of the human dopamine D3 receptor in complex with eticlopride
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044659 | biological_process | viral release from host cell by cytolysis |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0044659 | biological_process | viral release from host cell by cytolysis |
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 |
| A | ALA116-VAL132 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | ALA33-LEU55 | |
| B | ALA33-LEU55 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 88 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | LYS56-ASN65 | |
| A | ASP127-ARG149 | |
| A | ASN387-CYS400 | |
| B | LYS56-ASN65 | |
| B | ASP127-ARG149 | |
| B | ASN387-CYS400 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | TYR66-TYR88 | |
| B | TYR66-TYR88 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 90 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | LEU89-ASP104 | |
| A | GLY171-ASP187 | |
| A | ASN352-SER366 | |
| B | LEU89-ASP104 | |
| B | GLY171-ASP187 | |
| B | ASN352-SER366 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | VAL105-ILE126 | |
| B | VAL105-ILE126 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | VAL150-PHE170 | |
| B | VAL150-PHE170 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | PHE188-ALA209 | |
| B | PHE188-ALA209 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | MET330-LEU351 | |
| B | MET330-LEU351 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 38 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:21097933 |
| Chain | Residue | Details |
| A | ALA367-PHE386 | |
| B | ALA367-PHE386 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21097933, ECO:0007744|PDB:3PBL |
| Chain | Residue | Details |
| A | ASP110 | |
| A | PHE345 | |
| A | HIS349 | |
| B | ASP110 | |
| B | PHE345 | |
| B | HIS349 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN12 | |
| A | ASN19 | |
| A | ASN97 | |
| A | ASN173 | |
| B | ASN12 | |
| B | ASN19 | |
| B | ASN97 | |
| B | ASN173 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | GLU1011 | |
| B | GLU1011 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | ASP1020 | |
| B | ASP1020 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | LEU1032 | |
| A | PHE1104 | |
| B | LEU1032 | |
| B | PHE1104 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
| Chain | Residue | Details |
| A | SER1117 | |
| A | ASN1132 | |
| B | SER1117 | |
| B | ASN1132 |
