5G53
Structure of the adenosine A2A receptor bound to an engineered G protein
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 |
| 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 | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0016020 | cellular_component | membrane |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005525 | molecular_function | GTP binding |
| C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| C | 0019001 | molecular_function | guanyl nucleotide binding |
| C | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
| D | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| D | 0019001 | molecular_function | guanyl nucleotide binding |
| D | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
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 |
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 | 63 |
| 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 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 26 |
| Details | Region: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 9 |
| Details | Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 14 |
| Details | Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P04896","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P63096","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 5 |
| Details | Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
