Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004888 | molecular_function | transmembrane signaling receptor activity |
| A | 0007166 | biological_process | cell surface receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016020 | cellular_component | membrane |
| B | 0004888 | molecular_function | transmembrane signaling receptor activity |
| B | 0007166 | biological_process | cell surface receptor signaling pathway |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue 836 A 1201 |
| Chain | Residue |
| A | ASN219 |
| A | LYS395 |
| A | ARG400 |
| A | GLN477 |
| A | TRP480 |
| A | GLU481 |
| A | PHE484 |
| A | PRO513 |
| A | GLU518 |
| A | ASN521 |
| A | LEU522 |
| A | LEU221 |
| A | MET230 |
| A | TRP281 |
| A | ASP384 |
| A | VAL386 |
| A | SER387 |
| A | PHE391 |
| A | TYR394 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue FMN A 1202 |
| Chain | Residue |
| A | SER1010 |
| A | THR1011 |
| A | THR1012 |
| A | GLY1013 |
| A | ASN1014 |
| A | THR1015 |
| A | SER1058 |
| A | THR1059 |
| A | TRP1060 |
| A | GLY1061 |
| A | CYS1093 |
| A | GLY1094 |
| A | ASP1095 |
| A | TRP1098 |
| A | GLU1099 |
| A | TYR1100 |
| A | PHE1101 |
| A | CYS1102 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue 836 B 1201 |
| Chain | Residue |
| B | ASN219 |
| B | LEU221 |
| B | MET230 |
| B | ASP384 |
| B | VAL386 |
| B | PHE391 |
| B | TYR394 |
| B | LYS395 |
| B | ARG400 |
| B | GLN477 |
| B | TRP480 |
| B | GLU481 |
| B | PHE484 |
| B | PRO513 |
| B | GLU518 |
| B | ASN521 |
| B | LEU522 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue FMN B 1202 |
| Chain | Residue |
| B | SER1010 |
| B | THR1011 |
| B | THR1012 |
| B | GLY1013 |
| B | ASN1014 |
| B | THR1015 |
| B | SER1058 |
| B | THR1059 |
| B | TRP1060 |
| B | GLY1061 |
| B | CYS1093 |
| B | GLY1094 |
| B | ASP1095 |
| B | TRP1098 |
| B | TYR1100 |
| B | PHE1101 |
| B | CYS1102 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue OLC B 1203 |
| Chain | Residue |
| B | TRP339 |
| B | PHE343 |
| B | LEU346 |
| B | ILE445 |
| B | ASN446 |
| B | MET449 |
| B | LEU450 |
Functional Information from PROSITE/UniProt
| site_id | PS00201 |
| Number of Residues | 17 |
| Details | FLAVODOXIN Flavodoxin signature. IVYgSTtGnTEytAEtI |
| Chain | Residue | Details |
| A | ILE1006-ILE1022 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 282 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 58 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 206 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 40 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 232 |
| Details | Domain: {"description":"FZ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00090","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"35658032","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ZI0","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P56726","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P56726","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
