Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0010181 | molecular_function | FMN binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0010181 | molecular_function | FMN binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN A 149 |
| Chain | Residue |
| A | SER10 |
| A | SER93 |
| A | GLY94 |
| A | ASP95 |
| A | TYR98 |
| A | HIS100 |
| A | PHE101 |
| A | CYS102 |
| A | HOH160 |
| A | SER11 |
| A | THR12 |
| A | GLY13 |
| A | ASN14 |
| A | THR15 |
| A | SER58 |
| A | ALA59 |
| A | TRP60 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN B 150 |
| Chain | Residue |
| B | SER10 |
| B | SER11 |
| B | THR12 |
| B | GLY13 |
| B | ASN14 |
| B | THR15 |
| B | ALA28 |
| B | SER58 |
| B | ALA59 |
| B | TRP60 |
| B | GLY61 |
| B | SER93 |
| B | GLY94 |
| B | ASP95 |
| B | TYR98 |
| B | HIS100 |
| B | PHE101 |
| B | CYS102 |
| B | HOH151 |
| B | HOH301 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN C 151 |
| Chain | Residue |
| C | SER10 |
| C | SER11 |
| C | THR12 |
| C | GLY13 |
| C | ASN14 |
| C | THR15 |
| C | ALA28 |
| C | SER58 |
| C | ALA59 |
| C | TRP60 |
| C | GLY61 |
| C | SER93 |
| C | GLY94 |
| C | ASP95 |
| C | TYR98 |
| C | HIS100 |
| C | PHE101 |
| C | CYS102 |
| C | HOH169 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN D 152 |
| Chain | Residue |
| D | SER10 |
| D | SER11 |
| D | THR12 |
| D | GLY13 |
| D | ASN14 |
| D | THR15 |
| D | ALA28 |
| D | SER58 |
| D | ALA59 |
| D | TRP60 |
| D | GLY61 |
| D | SER93 |
| D | GLY94 |
| D | ASP95 |
| D | TYR98 |
| D | HIS100 |
| D | PHE101 |
| D | CYS102 |
| D | HOH153 |
Functional Information from PROSITE/UniProt
| site_id | PS00201 |
| Number of Residues | 17 |
| Details | FLAVODOXIN Flavodoxin signature. IVFgSStGnTEsiAQkL |
| Chain | Residue | Details |
| A | ILE6-LEU22 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 564 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]} |
