4AMJ
Turkey beta1 adrenergic receptor with stabilising mutations and bound biased agonist carvedilol
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 CVD A 1359 |
Chain | Residue |
A | TRP117 |
A | ASN329 |
A | TYR333 |
A | HOH2030 |
A | ASP121 |
A | PHE201 |
A | TYR207 |
A | SER211 |
A | SER215 |
A | PHE306 |
A | PHE307 |
A | ASN310 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 1360 |
Chain | Residue |
A | CYS192 |
A | ASP195 |
A | CYS198 |
A | HOH2014 |
A | HOH2015 |
A | HOH2028 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 2CV A 1361 |
Chain | Residue |
A | ARG157 |
A | VAL160 |
B | ARG205 |
B | 2CV1359 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE 2CV A 1362 |
Chain | Residue |
A | LEU289 |
A | GLY293 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE 2CV A 1363 |
Chain | Residue |
A | MET48 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 2CV A 1364 |
Chain | Residue |
A | TRP181 |
A | ASN204 |
A | TYR207 |
B | VAL160 |
B | THR164 |
B | 2CV1363 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 2CV A 1365 |
Chain | Residue |
A | ARG205 |
A | VAL314 |
A | PHE315 |
B | MET153 |
B | ARG157 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE 2CV A 1366 |
Chain | Residue |
A | MET179 |
A | TRP181 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE 2CV A 1367 |
Chain | Residue |
B | ARG157 |
B | ILE161 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE 2CV A 1368 |
Chain | Residue |
A | ARG148 |
B | PHE315 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 2CV B 1359 |
Chain | Residue |
A | VAL160 |
A | THR164 |
A | 2CV1361 |
B | PRO176 |
B | HIS180 |
B | TRP181 |
B | ASN204 |
site_id | BC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CVD B 1360 |
Chain | Residue |
B | LEU101 |
B | TRP117 |
B | ASP121 |
B | ASP200 |
B | PHE201 |
B | TYR207 |
B | SER211 |
B | SER215 |
B | TRP303 |
B | PHE306 |
B | PHE307 |
B | ASN310 |
B | ASN329 |
B | TYR333 |
B | HOH2020 |
B | HOH2038 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA B 1361 |
Chain | Residue |
B | CYS192 |
B | TYR193 |
B | ASP195 |
B | CYS198 |
B | HOH2016 |
B | HOH2033 |
B | HOH2034 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 2CV B 1362 |
Chain | Residue |
B | TYR231 |
B | HIS286 |
B | LEU289 |
B | MET296 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE 2CV B 1363 |
Chain | Residue |
A | TRP181 |
A | 2CV1364 |
B | TRP166 |
site_id | BC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE 2CV B 1364 |
Chain | Residue |
B | LEU308 |
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 | 56 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
A | GLN39-GLY67 | |
B | GLN39-GLY67 |
site_id | SWS_FT_FI2 |
Number of Residues | 156 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18594507 |
Chain | Residue | Details |
A | SER68-THR76 | |
A | ASP138-ARG155 | |
A | ARG232-ASN313 | |
B | SER68-THR76 | |
B | ASP138-ARG155 | |
B | ARG232-ASN313 |
site_id | SWS_FT_FI3 |
Number of Residues | 52 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
A | ASN77-VAL103 | |
B | ASN77-VAL103 |
site_id | SWS_FT_FI4 |
Number of Residues | 80 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:18594507 |
Chain | Residue | Details |
A | ARG104-GLU115 | |
A | HIS180-ARG205 | |
A | ASN316-VAL320 | |
B | ARG104-GLU115 | |
B | HIS180-ARG205 | |
B | ASN316-VAL320 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
A | LEU116-ILE137 | |
B | LEU116-ILE137 |
site_id | SWS_FT_FI6 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
A | ALA156-MET179 | |
B | ALA156-MET179 |
site_id | SWS_FT_FI7 |
Number of Residues | 50 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
A | ALA206-TYR231 | |
B | ALA206-TYR231 |
site_id | SWS_FT_FI8 |
Number of Residues | 58 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
A | HIS286-PHE315 | |
B | HIS286-PHE315 |
site_id | SWS_FT_FI9 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
A | PRO321-TYR343 | |
B | PRO321-TYR343 |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 |
Chain | Residue | Details |
A | ASP121 | |
A | SER211 | |
A | ASN329 | |
B | ASP121 | |
B | SER211 | |
B | ASN329 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250 |
Chain | Residue | Details |
A | ALA358 | |
B | ALA358 |