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 | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 64 |
| Details | Topological domain: {"description":"Cytoplasmic"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 74 |
| Details | Topological domain: {"description":"Extracellular"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D4S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17952055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RH1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8521811","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2540197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
