2RH1
High resolution crystal structure of human B2-adrenergic G protein-coupled receptor.
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 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 | CYS265 |
| 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 | GLU1011 |
| 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 | ASP1020 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
| Chain | Residue | Details |
| A | LEU1032 | |
| A | PHE1104 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
| Chain | Residue | Details |
| A | SER1117 | |
| A | ASN1132 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| A | GLU1011 | proton shuttle (general acid/base) |
| A | ASP1020 | covalent catalysis |
