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 | 22 |
Details | BINDING SITE FOR RESIDUE FNS A 570 |
Chain | Residue |
A | TYR143 |
A | THR280 |
A | LYS349 |
A | SER371 |
A | HIS373 |
A | GLY374 |
A | ARG376 |
A | ASP409 |
A | GLY410 |
A | GLY411 |
A | ARG413 |
A | TYR144 |
A | GLY432 |
A | ARG433 |
A | LEU436 |
A | SER195 |
A | ALA196 |
A | THR197 |
A | ALA198 |
A | SER228 |
A | GLN252 |
A | TYR254 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FNS B 571 |
Chain | Residue |
B | TYR143 |
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 |
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 |