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 | 48 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 56 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 34 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21593763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YDO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
