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 | 5 |
| Details | binding site for residue OLA A 501 |
| Chain | Residue |
| A | PHE71 |
| A | THR74 |
| A | OLA502 |
| A | CLR508 |
| A | CLR509 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue OLA A 502 |
| Chain | Residue |
| A | OLA501 |
| A | CLR509 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue OLA A 503 |
| Chain | Residue |
| A | CLR509 |
| A | PHE363 |
| A | CLR508 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue OLA A 504 |
| Chain | Residue |
| A | TYR52 |
| A | VAL55 |
| A | LEU67 |
| A | PHE88 |
| A | TRP138 |
| A | CLR508 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue OLA A 505 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 506 |
| Chain | Residue |
| A | ASP61 |
| A | SER100 |
| A | HOH610 |
| A | HOH637 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue ZMA A 507 |
| Chain | Residue |
| A | LEU94 |
| A | PHE177 |
| A | GLU178 |
| A | MET186 |
| A | TRP351 |
| A | LEU354 |
| A | HIS355 |
| A | ASN358 |
| A | MET375 |
| A | HOH631 |
| A | HOH643 |
| A | HOH645 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue CLR A 508 |
| Chain | Residue |
| A | ALA81 |
| A | ALA82 |
| A | ILE89 |
| A | OLA501 |
| A | OLA503 |
| A | OLA504 |
| A | CLR509 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue CLR A 509 |
| Chain | Residue |
| A | CYS359 |
| A | PHE360 |
| A | OLA501 |
| A | OLA502 |
| A | OLA503 |
| A | CLR508 |
| A | HOH626 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CLR A 510 |
| Chain | Residue |
| A | CYS367 |
| A | SER368 |
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 | SER99-ILE115 | |
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"}]} |
