8JJO
Cryo-EM structure of the beta2AR-mBRIL/1b3 Fab/Glue complex with an antagonist
Functional Information from GO Data
Chain | GOid | namespace | contents |
F | 0004930 | molecular_function | G protein-coupled receptor activity |
F | 0004935 | molecular_function | adrenergic receptor activity |
F | 0004941 | molecular_function | beta2-adrenergic receptor activity |
F | 0005506 | molecular_function | iron ion binding |
F | 0006940 | biological_process | regulation of smooth muscle contraction |
F | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
F | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
F | 0009055 | molecular_function | electron transfer activity |
F | 0016020 | cellular_component | membrane |
F | 0020037 | molecular_function | heme binding |
F | 0022900 | biological_process | electron transport chain |
F | 0042597 | cellular_component | periplasmic space |
F | 0097746 | biological_process | blood vessel diameter maintenance |
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. ASIeTLCVIAVDRYFaI |
Chain | Residue | Details |
F | ALA119-ILE135 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
F | GLY35-ILE58 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
F | ALA59-PHE71 | |
F | ASP130-ALA150 |
site_id | SWS_FT_FI3 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
F | ILE72-LEU95 |
site_id | SWS_FT_FI4 |
Number of Residues | 37 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
F | MET96-CYS106 | |
F | ARG175-ASN196 | |
F | GLN366-LYS372 |
site_id | SWS_FT_FI5 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
F | GLU107-VAL129 |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
F | ARG151-TYR174 |
site_id | SWS_FT_FI7 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
F | GLN197-SER220 |
site_id | SWS_FT_FI8 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
F | LEU342-ILE365 |
site_id | SWS_FT_FI9 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
F | GLU373-SER396 |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S |
Chain | Residue | Details |
F | ASP113 | |
F | THR118 | |
F | ASN360 | |
F | ASN379 | |
F | TYR383 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1 |
Chain | Residue | Details |
F | SER203 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811 |
Chain | Residue | Details |
F | TYR141 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000255 |
Chain | Residue | Details |
F | LEU329 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942 |
Chain | Residue | Details |
F | CYS332 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
F | TRP237 | |
F | ILE325 |