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 | 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 | 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 | 50 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 52 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 58 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| 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_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 | 4 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Site: {"description":"Deprotonates C-terminal active site Cys"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | Site: {"description":"Contributes to redox potential value"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
