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 | 20 |
| Details | binding site for residue EN6 A 1401 |
| Chain | Residue |
| A | PRO28 |
| A | PHE117 |
| A | TYR185 |
| A | HIS186 |
| A | ASP188 |
| A | ILE189 |
| A | PHE190 |
| A | GLU191 |
| A | PRO296 |
| A | SER299 |
| A | PHE300 |
| A | TYR34 |
| A | THR303 |
| A | ASP38 |
| A | VAL39 |
| A | CYS40 |
| A | THR44 |
| A | ILE47 |
| A | CYS94 |
| A | LEU101 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue FMN A 1402 |
| Chain | Residue |
| A | TYR140 |
| A | SER1010 |
| A | THR1011 |
| A | THR1012 |
| A | GLY1013 |
| A | ASN1014 |
| A | THR1015 |
| A | SER1058 |
| A | THR1059 |
| A | TRP1060 |
| A | GLY1061 |
| A | ASP1062 |
| A | CYS1093 |
| A | GLY1094 |
| A | ASP1095 |
| A | TRP1098 |
| A | TYR1100 |
| A | PHE1101 |
| A | CYS1102 |
| A | HOH1501 |
| A | HOH1505 |
| A | HOH1513 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1403 |
| Chain | Residue |
| A | THR82 |
| A | TRP166 |
| A | CYS170 |
| A | ASN295 |
| A | OLC1408 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 1404 |
| Chain | Residue |
| A | PHE89 |
| A | SER100 |
| A | GLU110 |
| A | THR113 |
| A | ARG269 |
| A | LEU298 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1405 |
| Chain | Residue |
| A | LEU112 |
| A | THR113 |
| A | ARG269 |
| A | SER272 |
| A | MET276 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 1406 |
| Chain | Residue |
| A | HIS103 |
| A | ALA213 |
| A | PHE217 |
| A | CYS220 |
| A | PHE221 |
| A | OLC1407 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1407 |
| Chain | Residue |
| A | HIS103 |
| A | OLC1406 |
| A | OLC1415 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1408 |
| Chain | Residue |
| A | GLY30 |
| A | ARG159 |
| A | TRP166 |
| A | THR297 |
| A | OLC1403 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 1409 |
| Chain | Residue |
| A | PHE177 |
| A | PHE178 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 1410 |
| Chain | Residue |
| A | GLY179 |
| A | TRP180 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 1411 |
| Chain | Residue |
| A | HIS73 |
| A | ARG139 |
| A | PHE227 |
| A | ARG231 |
| A | LYS1087 |
| A | ILE1148 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1412 |
| Chain | Residue |
| A | CYS134 |
| A | VAL137 |
| A | OLC1413 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 1413 |
| Chain | Residue |
| A | TRP130 |
| A | OLC1412 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue FLC A 1414 |
| Chain | Residue |
| A | VAL108 |
| A | ARG261 |
| A | ARG262 |
| A | MET265 |
| A | ARG269 |
| A | GLY1146 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1415 |
| Chain | Residue |
| A | VAL219 |
| A | CYS220 |
| A | PHE268 |
| A | TYR275 |
| A | OLC1407 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1416 |
| Chain | Residue |
| A | ARG269 |
| A | SER320 |
| A | LEU112 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue OLC A 1417 |
| Chain | Residue |
| A | PHE31 |
| A | HIS33 |
| A | VAL39 |
| A | ILE41 |
| A | PHE42 |
| A | GLU43 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1418 |
| Chain | Residue |
| A | LEU171 |
| A | PHE178 |
| A | TRP180 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue OLC A 1419 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1420 |
| Chain | Residue |
| A | THR60 |
| A | PHE63 |
| A | PEG1427 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 1421 |
| Chain | Residue |
| A | PHE42 |
| A | VAL46 |
| A | SER308 |
| site_id | AE4 |
| Number of Residues | 1 |
| Details | binding site for residue PEG A 1422 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1424 |
| Chain | Residue |
| A | ARG330 |
| A | ASP1106 |
| A | ARG1125 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 1426 |
| Chain | Residue |
| A | ASN150 |
| A | ASP1051 |
| A | ARG1086 |
| site_id | AE7 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 1427 |
| Chain | Residue |
| A | SER290 |
| A | OLC1420 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 1428 |
| Chain | Residue |
| A | GLN232 |
| A | HIS233 |
| A | THR234 |
| A | LYS235 |
| A | GLU236 |
Functional Information from PROSITE/UniProt
| site_id | PS00028 |
| Number of Residues | 23 |
| Details | ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cts..CmefLevlfqgphHhhhhhH |
| Chain | Residue | Details |
| A | CYS336-HIS358 | |
| 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"}]} |
