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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue QGW A 1201 |
| Chain | Residue |
| A | TYR9 |
| A | HIS250 |
| A | ASN253 |
| A | TYR271 |
| A | HOH1320 |
| A | ALA63 |
| A | ILE66 |
| A | SER67 |
| A | LEU85 |
| A | LEU167 |
| A | PHE168 |
| A | MET177 |
| A | LEU249 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 1202 |
| Chain | Residue |
| A | ASP52 |
| A | SER91 |
| A | ASN280 |
| A | HOH1338 |
| A | HOH1354 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CLR A 1203 |
| Chain | Residue |
| A | LEU247 |
| A | PRO248 |
| A | SER263 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CLR A 1204 |
| Chain | Residue |
| A | ALA72 |
| A | ALA73 |
| A | GLY76 |
| A | ILE80 |
| A | CLR1205 |
| A | OLB1206 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CLR A 1205 |
| Chain | Residue |
| A | PHE255 |
| A | CLR1204 |
| A | OLB1206 |
| A | OLA1215 |
| A | HOH1312 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue OLB A 1206 |
| Chain | Residue |
| A | PHE258 |
| A | CLR1204 |
| A | CLR1205 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1207 |
| Chain | Residue |
| A | CYS28 |
| A | VAL31 |
| A | TRP32 |
| A | VAL46 |
| A | ALA50 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1208 |
| Chain | Residue |
| A | THR65 |
| A | THR68 |
| A | PHE70 |
| A | OLA1215 |
| A | OLA1217 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue OLA A 1210 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue OLA A 1212 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue OLA A 1213 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue OLA A 1215 |
| Chain | Residue |
| A | CYS71 |
| A | CLR1205 |
| A | OLA1208 |
| A | OLA1217 |
| A | HOH1318 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1216 |
| Chain | Residue |
| A | GLY5 |
| A | TYR271 |
| A | HOH1345 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 1217 |
| Chain | Residue |
| A | PHE255 |
| A | CYS262 |
| A | OLA1208 |
| A | OLA1215 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 1218 |
| Chain | Residue |
| A | MET140 |
| A | LEU141 |
| A | TYR179 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1221 |
| Chain | Residue |
| A | TYR43 |
| A | ALA122 |
| A | TRP129 |
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 | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=1"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=2"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 46 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"18832607","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=3"} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=4"} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=5"} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=6"} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=7"} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21593763","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YDO","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
