5JQH
Structure of beta2 adrenoceptor bound to carazolol and inactive-state stabilizing nanobody, Nb60
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004941 | molecular_function | beta2-adrenergic receptor activity |
| A | 0006940 | biological_process | regulation of smooth muscle contraction |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044659 | biological_process | viral release from host cell by cytolysis |
| A | 0097746 | biological_process | blood vessel diameter maintenance |
| B | 0003796 | molecular_function | lysozyme activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004941 | molecular_function | beta2-adrenergic receptor activity |
| B | 0006940 | biological_process | regulation of smooth muscle contraction |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| B | 0009253 | biological_process | peptidoglycan catabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0030430 | cellular_component | host cell cytoplasm |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0042742 | biological_process | defense response to bacterium |
| B | 0044659 | biological_process | viral release from host cell by cytolysis |
| B | 0097746 | biological_process | blood vessel diameter maintenance |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue CAU A 1401 |
| Chain | Residue |
| A | ASP1113 |
| A | TYR1316 |
| A | VAL1114 |
| A | PHE1193 |
| A | SER1203 |
| A | SER1204 |
| A | TRP1286 |
| A | PHE1289 |
| A | PHE1290 |
| A | ASN1312 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CLR A 1402 |
| Chain | Residue |
| A | ILE1055 |
| A | VAL1081 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue CAU B 1401 |
| Chain | Residue |
| B | ASP1113 |
| B | VAL1114 |
| B | PHE1193 |
| B | SER1203 |
| B | PHE1289 |
| B | ASN1293 |
| B | TYR1308 |
| B | ASN1312 |
| B | TYR1316 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CLR B 1402 |
| Chain | Residue |
| B | ILE1055 |
| B | VAL1081 |
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. ASIeTLCVIAVDRYFaI |
| Chain | Residue | Details |
| A | ALA1119-ILE1135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | GLU876 | |
| B | GLU876 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | ASP885 | |
| B | ASP885 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | LEU897 | |
| A | PHE969 | |
| B | LEU897 | |
| B | PHE969 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
| Chain | Residue | Details |
| A | SER982 | |
| A | ASN997 | |
| B | SER982 | |
| B | ASN997 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=1 |
| Chain | Residue | Details |
| A | GLY1035-ILE1058 | |
| B | GLY1035-ILE1058 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 170 |
| Details | TOPO_DOM: Cytoplasmic |
| Chain | Residue | Details |
| A | ALA1059-PHE1071 | |
| A | ASP1130-ALA1150 | |
| A | ARG1221-ASP1300 | |
| B | ALA1059-PHE1071 | |
| B | ASP1130-ALA1150 | |
| B | ARG1221-ASP1300 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=2 |
| Chain | Residue | Details |
| A | ILE1072-LEU1095 | |
| B | ILE1072-LEU1095 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 74 |
| Details | TOPO_DOM: Extracellular |
| Chain | Residue | Details |
| A | THR1096-CYS1106 | |
| A | ARG1175-ASN1196 | |
| A | ILE1325-ASP1331 | |
| B | THR1096-CYS1106 | |
| B | ARG1175-ASN1196 | |
| B | ILE1325-ASP1331 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=3 |
| Chain | Residue | Details |
| A | GLU1107-VAL1129 | |
| B | GLU1107-VAL1129 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=4 |
| Chain | Residue | Details |
| A | ARG1151-TYR1174 | |
| B | ARG1151-TYR1174 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=5 |
| Chain | Residue | Details |
| A | GLN1197-SER1220 | |
| B | GLN1197-SER1220 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=6 |
| Chain | Residue | Details |
| A | ASN1301-LEU1324 | |
| B | ASN1301-LEU1324 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=7 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S |
| Chain | Residue | Details |
| A | ASP1113 | |
| B | LEU1342 | |
| A | THR1118 | |
| A | SER1319 | |
| A | GLU1338 | |
| A | LEU1342 | |
| B | ASP1113 | |
| B | THR1118 | |
| B | SER1319 | |
| B | GLU1338 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1 |
| Chain | Residue | Details |
| A | SER1203 | |
| B | SER1203 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811 |
| Chain | Residue | Details |
| A | TYR1141 | |
| B | TYR1141 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332 |
| Chain | Residue | Details |
| A | LEU1272 | |
| B | LEU1272 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000255 |
| Chain | Residue | Details |
| A | LEU1287 | |
| A | PRO1288 | |
| B | LEU1287 | |
| B | PRO1288 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942 |
| Chain | Residue | Details |
| A | ILE1291 | |
| B | ILE1291 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942 |
| Chain | Residue | Details |
