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 | 4 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 64 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 92 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
