Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 570 |
| Chain | Residue |
| A | TYR144 |
| A | LYS349 |
| A | SER371 |
| A | HIS373 |
| A | GLY374 |
| A | ARG376 |
| A | ASP409 |
| A | GLY410 |
| A | GLY411 |
| A | ARG413 |
| A | GLY432 |
| A | SER195 |
| A | ARG433 |
| A | LEU436 |
| A | EDO600 |
| A | HOH606 |
| A | ALA196 |
| A | THR197 |
| A | ALA198 |
| A | SER228 |
| A | GLN252 |
| A | TYR254 |
| A | THR280 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 600 |
| Chain | Residue |
| A | TYR143 |
| A | LEU230 |
| A | TYR254 |
| A | ARG289 |
| A | HIS373 |
| A | ARG376 |
| A | FMN570 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 670 |
| Chain | Residue |
| B | TYR144 |
| B | SER195 |
| B | ALA196 |
| B | THR197 |
| B | ALA198 |
| B | SER228 |
| B | GLN252 |
| B | TYR254 |
| B | THR280 |
| B | LYS349 |
| B | SER371 |
| B | HIS373 |
| B | GLY374 |
| B | ARG376 |
| B | ASP409 |
| B | GLY410 |
| B | GLY411 |
| B | ARG413 |
| B | GLY432 |
| B | ARG433 |
| B | LEU436 |
| B | EDO700 |
| B | HOH703 |
| B | HOH749 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 700 |
| Chain | Residue |
| B | TYR143 |
| B | TYR254 |
| B | ARG289 |
| B | HIS373 |
| B | ARG376 |
| B | FMN670 |
Functional Information from PROSITE/UniProt
| site_id | PS00557 |
| Number of Residues | 7 |
| Details | FMN_HYDROXY_ACID_DH_1 FMN-dependent alpha-hydroxy acid dehydrogenases active site. SNHGGRQ |
| Chain | Residue | Details |
| A | SER371-GLN377 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS373 | |
| B | HIS373 | |
| Chain | Residue | Details |
| A | GLN139 | |
| A | LYS296 | |
| B | GLN139 | |
| B | LYS296 | |
| Chain | Residue | Details |
| A | TYR143 | |
| A | ASP409 | |
| A | GLY432 | |
| B | TYR143 | |
| B | SER195 | |
| B | SER228 | |
| B | GLN252 | |
| B | TYR254 | |
| B | THR280 | |
| B | LYS349 | |
| B | HIS373 | |
| A | SER195 | |
| B | ARG376 | |
| B | ASP409 | |
| B | GLY432 | |
| A | SER228 | |
| A | GLN252 | |
| A | TYR254 | |
| A | THR280 | |
| A | LYS349 | |
| A | HIS373 | |
| A | ARG376 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | TYR254 | |
| A | TYR143 | |
| A | ARG376 | |
| A | ASP282 | |
| A | HIS373 | |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | TYR254 | |
| B | TYR143 | |
| B | ARG376 | |
| B | ASP282 | |
| B | HIS373 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| A | TYR254 | |
| A | ARG376 | |
| A | HIS373 | |
| A | ASP282 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1fcb |
| Chain | Residue | Details |
| B | TYR254 | |
| B | ARG376 | |
| B | HIS373 | |
| B | ASP282 | |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 102 |
| Chain | Residue | Details |
| A | TYR254 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP282 | electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS373 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 102 |
| Chain | Residue | Details |
| B | TYR254 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP282 | electrostatic stabiliser, hydrogen bond acceptor |
| B | HIS373 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
