Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0010181 | molecular_function | FMN binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0010181 | molecular_function | FMN binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0010181 | molecular_function | FMN binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0010181 | molecular_function | FMN binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 25 |
Details | binding site for residue FMN A 401 |
Chain | Residue |
A | ILE41 |
A | LYS241 |
A | SER263 |
A | HIS265 |
A | GLY266 |
A | ARG268 |
A | ASP296 |
A | SER297 |
A | GLY298 |
A | VAL299 |
A | ARG300 |
A | ALA92 |
A | GLY319 |
A | ARG320 |
A | PYR402 |
A | HOH517 |
A | HOH519 |
A | HOH579 |
A | PRO93 |
A | ILE94 |
A | ALA95 |
A | SER122 |
A | GLN144 |
A | TYR146 |
A | THR172 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue PYR A 402 |
Chain | Residue |
A | TYR40 |
A | ALA95 |
A | TYR124 |
A | TYR146 |
A | ARG181 |
A | TYR215 |
A | HIS265 |
A | ARG268 |
A | FMN401 |
site_id | AC3 |
Number of Residues | 24 |
Details | binding site for residue FMN B 401 |
Chain | Residue |
B | ILE41 |
B | PRO93 |
B | ILE94 |
B | ALA95 |
B | SER122 |
B | GLN144 |
B | TYR146 |
B | THR172 |
B | LYS241 |
B | SER263 |
B | HIS265 |
B | GLY266 |
B | ARG268 |
B | ASP296 |
B | SER297 |
B | GLY298 |
B | VAL299 |
B | ARG300 |
B | GLY319 |
B | ARG320 |
B | PYR402 |
B | HOH529 |
B | HOH538 |
B | HOH549 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue PYR B 402 |
Chain | Residue |
B | TYR40 |
B | ALA95 |
B | TYR124 |
B | TYR146 |
B | ARG181 |
B | LEU211 |
B | TYR215 |
B | HIS265 |
B | ARG268 |
B | FMN401 |
site_id | AC5 |
Number of Residues | 25 |
Details | binding site for residue FMN C 401 |
Chain | Residue |
C | TYR40 |
C | ILE41 |
C | ALA92 |
C | PRO93 |
C | ILE94 |
C | ALA95 |
C | SER122 |
C | GLN144 |
C | TYR146 |
C | THR172 |
C | LYS241 |
C | SER263 |
C | HIS265 |
C | GLY266 |
C | ARG268 |
C | ASP296 |
C | SER297 |
C | GLY298 |
C | ARG300 |
C | GLY319 |
C | ARG320 |
C | PYR402 |
C | HOH555 |
C | HOH585 |
C | HOH625 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue PYR C 402 |
Chain | Residue |
C | TYR215 |
C | HIS265 |
C | ARG268 |
C | FMN401 |
C | TYR40 |
C | ALA95 |
C | TYR124 |
C | TYR146 |
C | ARG181 |
C | LEU211 |
site_id | AC7 |
Number of Residues | 25 |
Details | binding site for residue FMN D 401 |
Chain | Residue |
D | TYR40 |
D | ILE41 |
D | ALA92 |
D | PRO93 |
D | ILE94 |
D | ALA95 |
D | SER122 |
D | GLN144 |
D | TYR146 |
D | THR172 |
D | LYS241 |
D | SER263 |
D | HIS265 |
D | GLY266 |
D | ARG268 |
D | ASP296 |
D | SER297 |
D | GLY298 |
D | ARG300 |
D | GLY319 |
D | ARG320 |
D | PYR402 |
D | HOH519 |
D | HOH526 |
D | HOH532 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue PYR D 402 |
Chain | Residue |
D | TYR40 |
D | TYR124 |
D | TYR146 |
D | ARG181 |
D | LEU211 |
D | TYR215 |
D | HIS265 |
D | ARG268 |
D | FMN401 |
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. SNHGARQ |
Chain | Residue | Details |
A | SER263-GLN269 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS265 | |
B | HIS265 | |
C | HIS265 | |
D | HIS265 | |
Chain | Residue | Details |
A | TYR40 | |
B | TYR215 | |
B | HIS265 | |
B | ARG268 | |
C | TYR40 | |
C | TYR146 | |
C | ARG181 | |
C | TYR215 | |
C | HIS265 | |
C | ARG268 | |
D | TYR40 | |
A | TYR146 | |
D | TYR146 | |
D | ARG181 | |
D | TYR215 | |
D | HIS265 | |
D | ARG268 | |
A | ARG181 | |
A | TYR215 | |
A | HIS265 | |
A | ARG268 | |
B | TYR40 | |
B | TYR146 | |
B | ARG181 | |
Chain | Residue | Details |
A | PRO93 | |
D | PRO93 | |
D | ASP296 | |
D | ARG320 | |
A | ASP296 | |
A | ARG320 | |
B | PRO93 | |
B | ASP296 | |
B | ARG320 | |
C | PRO93 | |
C | ASP296 | |
C | ARG320 | |
Chain | Residue | Details |
A | SER122 | |
C | THR172 | |
C | LYS241 | |
C | SER263 | |
D | SER122 | |
D | THR172 | |
D | LYS241 | |
D | SER263 | |
A | THR172 | |
A | LYS241 | |
A | SER263 | |
B | SER122 | |
B | THR172 | |
B | LYS241 | |
B | SER263 | |
C | SER122 | |
Chain | Residue | Details |
A | GLN144 | |
B | GLN144 | |
C | GLN144 | |
D | GLN144 | |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | SITE: Is suggested to participate in control of opening/closing motions of the active-site lid in A.viridans LOX => ECO:0000305|PubMed:27302031 |
Chain | Residue | Details |
A | TYR215 | |
B | TYR215 | |
C | TYR215 | |
D | TYR215 | |