8GGW
Locally refined cryoEM structure of receptor from beta-2-adrenergic receptor in complex with GTP-bound Gs heterotrimer (transition intermediate #15 of 20)
Functional Information from GO Data
Chain | GOid | namespace | contents |
R | 0004930 | molecular_function | G protein-coupled receptor activity |
R | 0004935 | molecular_function | adrenergic receptor activity |
R | 0004941 | molecular_function | beta2-adrenergic receptor activity |
R | 0006940 | biological_process | regulation of smooth muscle contraction |
R | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
R | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
R | 0016020 | cellular_component | membrane |
R | 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 |
R | ALA119-ILE135 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 70 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
R | MET-6-GLN27 | |
R | THR96-CYS106 | |
R | ARG175-ASN196 | |
R | GLN299-LYS305 |
site_id | SWS_FT_FI2 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
R | GLY35-ILE58 |
site_id | SWS_FT_FI3 |
Number of Residues | 168 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
R | ALA59-PHE71 | |
R | ASP130-ALA150 | |
R | ARG221-THR274 | |
R | PRO323-ASN406 |
site_id | SWS_FT_FI4 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
R | ILE72-LEU95 |
site_id | SWS_FT_FI5 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
R | GLU107-VAL129 |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
R | ARG151-TYR174 |
site_id | SWS_FT_FI7 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
R | GLN197-SER220 |
site_id | SWS_FT_FI8 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
R | LEU275-ILE298 |
site_id | SWS_FT_FI9 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
R | GLU306-SER329 |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S |
Chain | Residue | Details |
R | ASP113 | |
R | THR118 | |
R | ASN293 | |
R | ASN312 | |
R | TYR316 |
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 |
R | SER203 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811 |
Chain | Residue | Details |
R | TYR141 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332 |
Chain | Residue | Details |
R | SER246 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000255 |
Chain | Residue | Details |
R | SER261 | |
R | SER262 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000 |
Chain | Residue | Details |
R | SER345 | |
R | SER346 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by BARK => ECO:0000305 |
Chain | Residue | Details |
R | SER355 | |
R | SER356 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:19584355 |
Chain | Residue | Details |
R | PRO390 | |
R | PRO403 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942 |
Chain | Residue | Details |
R | CYS265 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942 |
Chain | Residue | Details |
R | CYS341 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305 |
Chain | Residue | Details |
R | ASN-1 | |
R | ASN8 |