Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0030168 | biological_process | platelet activation |
| A | 0043448 | biological_process | alkane catabolic process |
| A | 0045028 | molecular_function | G protein-coupled purinergic nucleotide receptor activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0090075 | biological_process | relaxation of muscle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue BUR A 1101 |
| Chain | Residue |
| A | PHE62 |
| A | OLC1107 |
| A | OLC1110 |
| A | OLC1113 |
| A | 1PE1114 |
| A | PHE66 |
| A | LEU102 |
| A | THR103 |
| A | PRO105 |
| A | ALA106 |
| A | MET123 |
| A | GLN127 |
| A | Y011105 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CLR A 1102 |
| Chain | Residue |
| A | PRO185 |
| A | TYR189 |
| A | SER213 |
| A | TYR217 |
| A | Y011103 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue Y01 A 1103 |
| Chain | Residue |
| A | ILE216 |
| A | CYS220 |
| A | ALA270 |
| A | MET279 |
| A | ARG301 |
| A | THR305 |
| A | CLR1102 |
| A | 1PE1114 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue Y01 A 1104 |
| Chain | Residue |
| A | TYR89 |
| A | CYS144 |
| A | HIS148 |
| A | ALA224 |
| A | LEU232 |
| A | TYR246 |
| A | LEU266 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue Y01 A 1105 |
| Chain | Residue |
| A | PHE62 |
| A | ILE108 |
| A | PHE109 |
| A | PHE112 |
| A | ASN113 |
| A | ARG301 |
| A | BUR1101 |
| A | OLC1113 |
| A | 1PE1114 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1106 |
| Chain | Residue |
| A | ARG212 |
| A | PHE215 |
| A | ILE216 |
| A | ASP289 |
| A | OLC1112 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue OLC A 1107 |
| Chain | Residue |
| A | PHE109 |
| A | SER184 |
| A | PHE188 |
| A | TYR189 |
| A | TYR210 |
| A | SER213 |
| A | ARG301 |
| A | BUR1101 |
| A | 1PE1114 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1108 |
| Chain | Residue |
| A | ASP121 |
| A | PHE129 |
| A | OLC1110 |
| A | HOH1206 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 1109 |
| Chain | Residue |
| A | LYS46 |
| A | PHE49 |
| A | TYR53 |
| A | PHE112 |
| A | CYS318 |
| A | OLC1111 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue OLC A 1110 |
| Chain | Residue |
| A | ILE118 |
| A | PHE119 |
| A | ASP121 |
| A | MET123 |
| A | LYS125 |
| A | SER184 |
| A | LEU187 |
| A | PHE188 |
| A | BUR1101 |
| A | OLC1108 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 1111 |
| Chain | Residue |
| A | PHE51 |
| A | TYR52 |
| A | PRO55 |
| A | TYR111 |
| A | PHE112 |
| A | OLC1109 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1112 |
| Chain | Residue |
| A | PHE226 |
| A | THR281 |
| A | MET282 |
| A | ARG285 |
| A | OLC1106 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue OLC A 1113 |
| Chain | Residue |
| A | THR267 |
| A | ALA270 |
| A | ARG301 |
| A | THR305 |
| A | VAL308 |
| A | BUR1101 |
| A | Y011105 |
| A | 1PE1114 |
| A | HOH1217 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE A 1114 |
| Chain | Residue |
| A | Y011105 |
| A | OLC1107 |
| A | OLC1113 |
| A | ARG301 |
| A | BUR1101 |
| A | Y011103 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 1115 |
| Chain | Residue |
| A | CYS1006 |
| A | CYS1009 |
| A | CYS1039 |
| A | CYS1042 |
Functional Information from PROSITE/UniProt
| site_id | PS00202 |
| Number of Residues | 11 |
| Details | RUBREDOXIN Rubredoxin signature. IpDDWvCPlCG |
| Chain | Residue | Details |
| A | ILE1033-GLY1043 | |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. GSIlFLTCISAHRYSgV |
| Chain | Residue | Details |
| A | GLY137-VAL153 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 58 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4XNW","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |