2VT4
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND CYANOPINDOLOL
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004935 | molecular_function | adrenergic receptor activity |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0016020 | cellular_component | membrane |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004935 | molecular_function | adrenergic receptor activity |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0016020 | cellular_component | membrane |
| C | 0004930 | molecular_function | G protein-coupled receptor activity |
| C | 0004935 | molecular_function | adrenergic receptor activity |
| C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| C | 0016020 | cellular_component | membrane |
| D | 0004930 | molecular_function | G protein-coupled receptor activity |
| D | 0004935 | molecular_function | adrenergic receptor activity |
| D | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| D | 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. ASIeTLCVIAIDRYLaI |
| Chain | Residue | Details |
| A | ALA127-ILE143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 100 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 104 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 160 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 84 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 92 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 100 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 116 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 88 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2VT4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 56 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| Chain | Residue | Details |
