4AMI
Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist bucindolol
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 | 0004940 | molecular_function | beta1-adrenergic receptor activity |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| A | 0016020 | cellular_component | membrane |
| A | 0045823 | biological_process | positive regulation of heart contraction |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004935 | molecular_function | adrenergic receptor activity |
| B | 0004940 | molecular_function | beta1-adrenergic receptor activity |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| B | 0016020 | cellular_component | membrane |
| B | 0045823 | biological_process | positive regulation of heart contraction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE G90 A 1359 |
| Chain | Residue |
| A | TRP117 |
| A | PHE306 |
| A | ASN310 |
| A | ASN329 |
| A | ASP121 |
| A | VAL122 |
| A | VAL125 |
| A | CYS199 |
| A | PHE201 |
| A | SER211 |
| A | SER215 |
| A | TRP303 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 2CV A 1360 |
| Chain | Residue |
| A | ARG183 |
| A | ASN204 |
| A | TYR207 |
| B | THR164 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 2CV B 1358 |
| Chain | Residue |
| B | ILE214 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 2CV B 1359 |
| Chain | Residue |
| A | ARG157 |
| B | ARG205 |
| B | 2CV1361 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE G90 B 1360 |
| Chain | Residue |
| B | TRP117 |
| B | ASP121 |
| B | VAL122 |
| B | VAL125 |
| B | CYS199 |
| B | ASP200 |
| B | SER211 |
| B | SER215 |
| B | TRP303 |
| B | PHE306 |
| B | ASN329 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 2CV B 1361 |
| Chain | Residue |
| A | VAL160 |
| A | THR164 |
| B | ARG183 |
| B | ASP184 |
| B | GLU185 |
| B | 2CV1359 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE 2CV B 1362 |
| Chain | Residue |
| B | ILE161 |
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 | 46 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 68 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 38 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| 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_FI11 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P08588","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
