8GGI
Locally refined cryoEM structure of receptor from beta-2-adrenergic receptor in complex with GTP-bound Gs heterotrimer (transition intermediate #1 of 20)
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 | THR96-CYS106 | |
| R | ARG175-ASN196 | |
| R | GLN299-LYS305 | |
| R | MET-6-GLN27 |
| 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 |
