8GNG
Crystal structure of human adenosine A2A receptor in complex with istradefylline.
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 | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0016020 | cellular_component | membrane |
| X | 0001609 | molecular_function | G protein-coupled adenosine receptor activity |
| X | 0001973 | biological_process | G protein-coupled adenosine receptor signaling pathway |
| X | 0004930 | molecular_function | G protein-coupled receptor activity |
| X | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| X | 0016020 | cellular_component | membrane |
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. SSIfSLLAIAIDRYIaI |
| Chain | Residue | Details |
| A | SER90-ILE106 |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| L | TYR192-HIS198 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 104 |
| Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:18832607 |
| Chain | Residue | Details |
| A | MET1-SER7 | |
| A | SER67-CYS77 | |
| A | ASN144-PRO173 | |
| A | CYS259-PRO266 | |
| X | MET1-SER7 | |
| X | SER67-CYS77 | |
| X | ASN144-PRO173 | |
| X | CYS259-PRO266 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | TRANSMEM: Helical; Name=1 |
| Chain | Residue | Details |
| A | VAL8-TRP32 | |
| X | VAL8-TRP32 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 126 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18832607 |
| Chain | Residue | Details |
| A | LEU33-ASN42 | |
| A | ASP101-ARG120 | |
| A | ARG199-SER234 | |
| X | LEU33-ASN42 | |
| X | ASP101-ARG120 | |
| X | ARG199-SER234 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=2 |
| Chain | Residue | Details |
| A | TYR43-ILE66 | |
| X | TYR43-ILE66 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=3 |
| Chain | Residue | Details |
| A | LEU78-ILE100 | |
| X | LEU78-ILE100 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=4 |
| Chain | Residue | Details |
| A | ALA121-TRP143 | |
| X | ALA121-TRP143 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 48 |
| Details | TRANSMEM: Helical; Name=5 |
| Chain | Residue | Details |
| A | MET174-LEU198 | |
| X | MET174-LEU198 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=6 |
| Chain | Residue | Details |
| A | LEU235-PHE258 | |
| X | LEU235-PHE258 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=7 |
| Chain | Residue | Details |
| A | LEU267-TYR290 | |
| X | LEU267-TYR290 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21593763, ECO:0007744|PDB:2YDO |
| Chain | Residue | Details |
| A | GLU169 | |
| A | ASN253 | |
| A | SER277 | |
| A | HIS278 | |
| X | GLU169 | |
| X | ASN253 | |
| X | SER277 | |
| X | HIS278 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | GLN154 | |
| X | GLN154 |
