2Y03
TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND AGONIST ISOPRENALINE
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 | 9 |
| Details | BINDING SITE FOR RESIDUE Y01 A 401 |
| Chain | Residue |
| A | GLU130 |
| A | ARG157 |
| A | ILE161 |
| A | THR164 |
| A | HOH2007 |
| B | ARG205 |
| B | ILE209 |
| B | ALA210 |
| B | Y01401 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 2CV A 501 |
| Chain | Residue |
| A | HIS180 |
| A | TRP181 |
| A | ASP184 |
| A | GLU185 |
| A | ASN204 |
| A | ALA206 |
| B | VAL160 |
| B | THR164 |
| B | Y01401 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 2CV A 502 |
| Chain | Residue |
| A | VAL230 |
| A | GLY293 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 2CV A 503 |
| Chain | Residue |
| A | ARG205 |
| A | PHE315 |
| B | ARG148 |
| B | ARG157 |
| B | Y01401 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 5FW A 601 |
| Chain | Residue |
| A | ASP121 |
| A | SER211 |
| A | SER215 |
| A | PHE306 |
| A | PHE307 |
| A | ASN329 |
| A | TYR333 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 701 |
| Chain | Residue |
| A | CYS192 |
| A | TYR193 |
| A | ASP195 |
| A | CYS198 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE Y01 B 401 |
| Chain | Residue |
| A | ALA206 |
| A | Y01401 |
| A | 2CV501 |
| A | 2CV503 |
| B | GLU130 |
| B | ARG157 |
| B | ILE161 |
| B | THR164 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 2CV B 501 |
| Chain | Residue |
| A | VAL160 |
| A | THR164 |
| B | ARG183 |
| B | ASP184 |
| B | GLU185 |
| B | TYR207 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 2CV B 502 |
| Chain | Residue |
| B | VAL230 |
| B | MET296 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 2CV B 503 |
| Chain | Residue |
| A | ARG157 |
| B | ARG205 |
| B | VAL314 |
| B | PHE315 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 5FW B 601 |
| Chain | Residue |
| B | TRP117 |
| B | ASP121 |
| B | VAL122 |
| B | SER211 |
| B | SER215 |
| B | PHE306 |
| B | ASN310 |
| B | ASN329 |
| B | TYR333 |
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 | Transmembrane: {"description":"Helical; Name=1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 50 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 52 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 80 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18594507","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 58 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| 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 | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
