8WCC
Cryo-EM structure of the CHA-bound mTAAR1 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
R | 0001594 | molecular_function | trace-amine receptor activity |
R | 0004930 | molecular_function | G protein-coupled receptor activity |
R | 0005783 | cellular_component | endoplasmic reticulum |
R | 0005789 | cellular_component | endoplasmic reticulum membrane |
R | 0005886 | cellular_component | plasma membrane |
R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
R | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
R | 0007191 | biological_process | adenylate cyclase-activating dopamine receptor signaling pathway |
R | 0007193 | biological_process | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway |
R | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
R | 0008227 | molecular_function | G protein-coupled amine receptor activity |
R | 0012505 | cellular_component | endomembrane system |
R | 0016020 | cellular_component | membrane |
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. ASIfHLAFISIDRYCaV |
Chain | Residue | Details |
R | ALA108-VAL124 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 60 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | MET1-ALA23 | |
R | GLU161-LYS187 | |
R | ASP271-ASN283 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | SER24-SER48 |
site_id | SWS_FT_FI3 |
Number of Residues | 90 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | HIS49-ASN58 | |
R | ASP119-THR138 | |
R | ARG211-ALA246 | |
R | TYR305-LEU332 |
site_id | SWS_FT_FI4 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | TRP59-MET80 |
site_id | SWS_FT_FI5 |
Number of Residues | 14 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465, ECO:0000305 |
Chain | Residue | Details |
R | VAL81-CYS95 |
site_id | SWS_FT_FI6 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | LYS96-ILE118 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | ILE139-LEU160 |
site_id | SWS_FT_FI8 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | VAL188-TYR210 |
site_id | SWS_FT_FI9 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | ALA247-LEU270 |
site_id | SWS_FT_FI10 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:37935376, ECO:0000269|PubMed:37963465 |
Chain | Residue | Details |
R | ASP284-PHE304 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:37963465, ECO:0007744|PDB:8WC6 |
Chain | Residue | Details |
R | ASP102 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
R | ASN9 |