6IBL
ACTIVATED TURKEY BETA1 ADRENOCEPTOR WITH BOUND AGONIST FORMOTEROL AND NANOBODY Nb80
Replaces: 6H7KFunctional 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 | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
A | 0015035 | molecular_function | protein-disulfide reductase activity |
A | 0015036 | molecular_function | disulfide oxidoreductase activity |
A | 0016020 | cellular_component | membrane |
A | 0030337 | molecular_function | DNA polymerase processivity factor activity |
A | 0045454 | biological_process | cell redox homeostasis |
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 | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
B | 0015035 | molecular_function | protein-disulfide reductase activity |
B | 0015036 | molecular_function | disulfide oxidoreductase activity |
B | 0016020 | cellular_component | membrane |
B | 0030337 | molecular_function | DNA polymerase processivity factor activity |
B | 0045454 | biological_process | cell redox homeostasis |
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 H98 A 501 |
Chain | Residue |
A | ASP121 |
A | ASN310 |
A | ASN329 |
A | TYR333 |
A | VAL125 |
A | CYS199 |
A | ASP200 |
A | PHE201 |
A | ALA208 |
A | SER211 |
A | SER215 |
A | PHE306 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue NA A 502 |
Chain | Residue |
A | CYS192 |
A | ASP195 |
A | CYS198 |
A | HOH608 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue 2CV A 503 |
Chain | Residue |
A | LEU171 |
A | TRP181 |
A | ASN204 |
A | ALA206 |
A | TYR207 |
A | ALA210 |
B | VAL60 |
B | ILE63 |
B | ALA64 |
B | GLY67 |
B | SER68 |
B | LEU92 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue 2CV A 504 |
Chain | Residue |
A | GLU130 |
A | ARG157 |
A | VAL160 |
A | THR164 |
B | PHE97 |
B | ARG104 |
B | TRP109 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue 2CV A 505 |
Chain | Residue |
A | THR81 |
A | CYS85 |
A | LEU120 |
A | LYS159 |
A | ILE162 |
A | CYS163 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue 2CV A 506 |
Chain | Residue |
A | LEU220 |
A | LEU289 |
A | LYS290 |
A | THR300 |
A | LEU304 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue 2CV A 507 |
Chain | Residue |
A | ALA206 |
A | ILE209 |
B | ILE63 |
B | THR81 |
B | LEU93 |
B | 2CV504 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue H98 B 501 |
Chain | Residue |
B | ASP121 |
B | VAL125 |
B | CYS199 |
B | ASP200 |
B | PHE201 |
B | ALA208 |
B | SER211 |
B | SER215 |
B | PHE306 |
B | ASN310 |
B | ASN329 |
B | TYR333 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue NA B 502 |
Chain | Residue |
B | CYS192 |
B | ASP195 |
B | CYS198 |
B | HOH608 |
B | HOH611 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue 2CV B 503 |
Chain | Residue |
B | LEU289 |
B | GLY293 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue 2CV B 504 |
Chain | Residue |
A | ARG205 |
A | 2CV507 |
B | LEU78 |
B | THR81 |
B | SER82 |
B | LYS159 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue 2CV B 505 |
Chain | Residue |
B | PHE174 |
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 | 4 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | SER1032 | |
A | SER1035 | |
B | SER1032 | |
B | SER1035 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: Deprotonates C-terminal active site Cys |
Chain | Residue | Details |
A | ASP1026 | |
B | ASP1026 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Contributes to redox potential value |
Chain | Residue | Details |
A | GLY1033 | |
A | PRO1034 | |
B | GLY1033 | |
B | PRO1034 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS1069 | |
B | LYS1069 |
site_id | SWS_FT_FI5 |
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_FI6 |
Number of Residues | 52 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
A | ASN77-VAL103 | |
B | ASN77-VAL103 |
site_id | SWS_FT_FI7 |
Number of Residues | 80 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:18594507 |
Chain | Residue | Details |
A | ARG104-GLU115 | |
A | HIS180-ARG205 | |
A | CYS344-ASP348 | |
B | ARG104-GLU115 | |
B | HIS180-ARG205 | |
B | CYS344-ASP348 |
site_id | SWS_FT_FI8 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
A | LEU116-ILE137 | |
B | LEU116-ILE137 |
site_id | SWS_FT_FI9 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
A | ALA156-MET179 | |
B | ALA156-MET179 |
site_id | SWS_FT_FI10 |
Number of Residues | 50 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
A | ALA206-TYR231 | |
B | ALA206-TYR231 |
site_id | SWS_FT_FI11 |
Number of Residues | 58 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
A | VAL314-TYR343 | |
B | VAL314-TYR343 |
site_id | SWS_FT_FI12 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
A | PHE349-HIS371 | |
B | PHE349-HIS371 |
site_id | SWS_FT_FI13 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 |
Chain | Residue | Details |
A | ASP121 | |
A | SER211 | |
A | LEU357 | |
B | ASP121 | |
B | SER211 | |
B | LEU357 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000250 |
Chain | Residue | Details |