3P0G
Structure of a nanobody-stabilized active state of the beta2 adrenoceptor
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 | 0008152 | biological_process | metabolic process |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE P0G A 366 |
Chain | Residue |
A | TRP109 |
A | PHE290 |
A | ASN293 |
A | TYR308 |
A | ILE309 |
A | ASN312 |
A | ASP113 |
A | VAL117 |
A | CYS191 |
A | PHE193 |
A | ALA200 |
A | SER203 |
A | SER207 |
A | PHE289 |
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 | ALA119-ILE135 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 70 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
A | MET1-VAL34 | |
A | MET96-CYS106 | |
A | ARG175-ASN196 | |
A | GLN299-LYS305 |
site_id | SWS_FT_FI2 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=1 |
Chain | Residue | Details |
A | GLY35-ILE58 |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
A | ALA59-PHE71 | |
A | ASP130-ALA150 |
site_id | SWS_FT_FI4 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=2 |
Chain | Residue | Details |
A | ILE72-LEU95 |
site_id | SWS_FT_FI5 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=3 |
Chain | Residue | Details |
A | GLU107-VAL129 |
site_id | SWS_FT_FI6 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=4 |
Chain | Residue | Details |
A | ARG151-TYR174 |
site_id | SWS_FT_FI7 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=5 |
Chain | Residue | Details |
A | GLN197-SER220 |
site_id | SWS_FT_FI8 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=6 |
Chain | Residue | Details |
A | LEU275-ILE298 |
site_id | SWS_FT_FI9 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=7 |
Chain | Residue | Details |
A | GLU306-SER329 |
site_id | SWS_FT_FI10 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S |
Chain | Residue | Details |
A | ASP113 | |
A | THR118 | |
A | ASN293 | |
A | ASN312 | |
A | TYR316 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1 |
Chain | Residue | Details |
A | SER203 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811 |
Chain | Residue | Details |
A | TYR141 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000 |
Chain | Residue | Details |
A | SER345 | |
A | SER346 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by BARK => ECO:0000305 |
Chain | Residue | Details |
A | SER355 | |
A | SER356 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942 |
Chain | Residue | Details |
A | CYS233 |
site_id | SWS_FT_FI16 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942 |
Chain | Residue | Details |
A | CYS341 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305 |
Chain | Residue | Details |
A | ASN6 | |
A | ASN15 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
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 | GLU227 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
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 | ASP227 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU228 | |
A | PHE231 |
site_id | SWS_FT_FI21 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER231 | |
A | ASN232 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 921 |
Chain | Residue | Details |
A | GLU227 | proton shuttle (general acid/base) |
A | ASP227 | covalent catalysis |