Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue FMN A 1202 |
| Chain | Residue |
| A | SER1010 |
| A | GLY1061 |
| A | CYS1093 |
| A | GLY1094 |
| A | ASP1095 |
| A | TRP1098 |
| A | TYR1100 |
| A | PHE1101 |
| A | CYS1102 |
| A | THR1011 |
| A | THR1012 |
| A | GLY1013 |
| A | ASN1014 |
| A | THR1015 |
| A | SER1058 |
| A | THR1059 |
| A | TRP1060 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1203 |
| Chain | Residue |
| A | THR75 |
| A | PRO155 |
| A | LEU158 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue OLC A 1204 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PGE A 1205 |
| Chain | Residue |
| A | PHE65 |
| A | TYR263 |
| A | TYR317 |
| A | ASP321 |
| A | PHE324 |
Functional Information from PROSITE/UniProt
| site_id | PS00201 |
| Number of Residues | 17 |
| Details | FLAVODOXIN Flavodoxin signature. IVYgSTtGnTEytAEtI |
| Chain | Residue | Details |
| A | ILE1006-ILE1022 | |
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. VSMwCLACISVDRYLaI |
| Chain | Residue | Details |
| A | VAL127-ILE143 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 141 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 42 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 38 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
