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 |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0010181 | molecular_function | FMN binding |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0010181 | molecular_function | FMN binding |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0010181 | molecular_function | FMN binding |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0010181 | molecular_function | FMN binding |
| H | 0009055 | molecular_function | electron transfer activity |
| H | 0010181 | molecular_function | FMN binding |
| I | 0009055 | molecular_function | electron transfer activity |
| I | 0010181 | molecular_function | FMN binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN A 149 |
| Chain | Residue |
| A | SER10 |
| A | GLY61 |
| A | SER93 |
| A | GLY94 |
| A | ASP95 |
| A | TYR98 |
| A | HIS100 |
| A | PHE101 |
| A | CYS102 |
| G | ALA138 |
| G | SER139 |
| A | SER11 |
| G | GLU142 |
| A | THR12 |
| A | GLY13 |
| A | ASN14 |
| A | THR15 |
| A | SER58 |
| A | ALA59 |
| A | TRP60 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN B 150 |
| Chain | Residue |
| A | ALA138 |
| A | SER139 |
| A | GLU142 |
| B | SER10 |
| B | SER11 |
| B | THR12 |
| B | GLY13 |
| B | ASN14 |
| B | THR15 |
| B | SER58 |
| B | ALA59 |
| B | TRP60 |
| B | GLY61 |
| B | SER93 |
| B | GLY94 |
| B | ASP95 |
| B | TYR98 |
| B | HIS100 |
| B | PHE101 |
| B | CYS102 |
| B | HOH161 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN D 151 |
| Chain | Residue |
| D | SER10 |
| D | SER11 |
| D | THR12 |
| D | GLY13 |
| D | ASN14 |
| D | THR15 |
| D | SER58 |
| D | ALA59 |
| D | TRP60 |
| D | GLY61 |
| D | MET62 |
| D | SER93 |
| D | GLY94 |
| D | ASP95 |
| D | TYR98 |
| D | HIS100 |
| D | PHE101 |
| D | CYS102 |
| D | HOH154 |
| F | ILE119 |
| F | ALA121 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN E 152 |
| Chain | Residue |
| B | SER139 |
| B | GLU142 |
| E | SER10 |
| E | SER11 |
| E | THR12 |
| E | GLY13 |
| E | ASN14 |
| E | THR15 |
| E | SER58 |
| E | ALA59 |
| E | TRP60 |
| E | GLY61 |
| E | SER93 |
| E | GLY94 |
| E | ASP95 |
| E | TYR98 |
| E | HIS100 |
| E | PHE101 |
| E | CYS102 |
| E | HOH163 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN F 153 |
| Chain | Residue |
| F | HOH150 |
| I | ILE119 |
| I | ILE120 |
| I | ALA121 |
| F | SER10 |
| F | SER11 |
| F | THR12 |
| F | GLY13 |
| F | ASN14 |
| F | THR15 |
| F | SER58 |
| F | ALA59 |
| F | TRP60 |
| F | GLY61 |
| F | SER93 |
| F | GLY94 |
| F | ASP95 |
| F | TYR98 |
| F | HIS100 |
| F | PHE101 |
| F | CYS102 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN H 154 |
| Chain | Residue |
| D | LYS113 |
| D | ILE119 |
| D | ILE120 |
| D | ALA121 |
| H | SER10 |
| H | SER11 |
| H | THR12 |
| H | GLY13 |
| H | ASN14 |
| H | THR15 |
| H | SER58 |
| H | ALA59 |
| H | TRP60 |
| H | GLY61 |
| H | SER93 |
| H | GLY94 |
| H | ASP95 |
| H | TYR98 |
| H | HIS100 |
| H | PHE101 |
| H | CYS102 |
| H | HOH149 |
| H | HOH151 |
| site_id | AC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN I 155 |
| Chain | Residue |
| H | ILE119 |
| H | ILE120 |
| H | ALA121 |
| I | SER10 |
| I | SER11 |
| I | THR12 |
| I | GLY13 |
| I | ASN14 |
| I | THR15 |
| I | SER58 |
| I | ALA59 |
| I | TRP60 |
| I | GLY61 |
| I | MET62 |
| I | SER93 |
| I | GLY94 |
| I | ASP95 |
| I | TYR98 |
| I | HIS100 |
| I | PHE101 |
| I | CYS102 |
| I | HOH150 |
| I | HOH168 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN G 156 |
| Chain | Residue |
| E | ALA138 |
| E | SER139 |
| E | GLU142 |
| G | SER10 |
| G | SER11 |
| G | THR12 |
| G | GLY13 |
| G | ASN14 |
| G | THR15 |
| G | SER58 |
| G | ALA59 |
| G | TRP60 |
| G | GLY61 |
| G | SER93 |
| G | GLY94 |
| G | ASP95 |
| G | TYR98 |
| G | HIS100 |
| G | PHE101 |
| G | CYS102 |
| G | HOH172 |
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 | 1128 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]} |