5UEN
Crystal structure of the human adenosine A1 receptor A1AR-bRIL in complex with the covalent antagonist DU172 at 3.2A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001609 | molecular_function | G protein-coupled adenosine receptor activity |
A | 0001973 | biological_process | G protein-coupled adenosine receptor signaling pathway |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
B | 0001609 | molecular_function | G protein-coupled adenosine receptor activity |
B | 0001973 | biological_process | G protein-coupled adenosine receptor signaling pathway |
B | 0004930 | molecular_function | G protein-coupled receptor activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0009055 | molecular_function | electron transfer activity |
B | 0016020 | cellular_component | membrane |
B | 0020037 | molecular_function | heme binding |
B | 0022900 | biological_process | electron transport chain |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue DU1 A 1201 |
Chain | Residue |
A | TYR12 |
A | LEU250 |
A | ASN254 |
A | TYR271 |
A | ILE274 |
A | ASN70 |
A | VAL87 |
A | LEU88 |
A | THR91 |
A | PHE171 |
A | GLU172 |
A | MET180 |
A | TRP247 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1202 |
Chain | Residue |
A | ALA125 |
A | VAL137 |
A | PHE144 |
A | OLA1203 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1203 |
Chain | Residue |
A | CYS46 |
A | VAL49 |
A | ILE89 |
A | OLA1202 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue OLA A 1204 |
Chain | Residue |
A | ILE5 |
A | ALA7 |
A | LEU18 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue OLA A 1205 |
Chain | Residue |
A | PHE8 |
A | ASN70 |
A | ILE268 |
A | TYR271 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue DU1 B 1201 |
Chain | Residue |
B | TYR12 |
B | VAL87 |
B | LEU88 |
B | THR91 |
B | PHE171 |
B | MET180 |
B | TRP247 |
B | LEU250 |
B | ASN254 |
B | TYR271 |
B | ILE274 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue OLA B 1202 |
Chain | Residue |
B | ALA125 |
B | PHE136 |
B | VAL137 |
B | OLA1203 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue OLA B 1203 |
Chain | Residue |
B | VAL49 |
B | ILE89 |
B | TRP132 |
B | OLA1202 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue OLA B 1204 |
Chain | Residue |
B | ALA10 |
B | VAL17 |
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. SSIlALLAIAVDRYLrV |
Chain | Residue | Details |
A | SER93-VAL109 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | ALA11-ALA33 | |
B | ALA11-ALA33 |
site_id | SWS_FT_FI2 |
Number of Residues | 64 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | VAL34-CYS46 | |
A | VAL103-ARG123 | |
B | VAL34-CYS46 | |
B | VAL103-ARG123 |
site_id | SWS_FT_FI3 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | PHE47-ILE69 | |
B | PHE47-ILE69 |
site_id | SWS_FT_FI4 |
Number of Residues | 92 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | ASN70-CYS80 | |
A | ASN147-SER176 | |
A | CYS260-SER267 | |
B | ASN70-CYS80 | |
B | ASN147-SER176 | |
B | CYS260-SER267 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
A | LEU81-ALA102 | |
B | LEU81-ALA102 |
site_id | SWS_FT_FI6 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
A | ALA124-TRP146 | |
B | ALA124-TRP146 |
site_id | SWS_FT_FI7 |
Number of Residues | 48 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
A | MET177-LEU201 | |
B | MET177-LEU201 |
site_id | SWS_FT_FI8 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
A | LEU236-PHE259 | |
B | LEU236-PHE259 |
site_id | SWS_FT_FI9 |
Number of Residues | 48 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
A | ILE268-ILE292 | |
B | ILE268-ILE292 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000255 |
Chain | Residue | Details |
A | CYS309 | |
B | CYS309 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ALA159 | |
B | ALA159 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP1007 | |
A | ILE1102 | |
B | TRP1007 | |
B | ILE1102 |