Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
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 | 0004459 | molecular_function | L-lactate dehydrogenase activity |
B | 0010181 | molecular_function | FMN binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN A 375 |
Chain | Residue |
A | ILE41 |
A | LYS241 |
A | SER263 |
A | HIS265 |
A | GLY266 |
A | ARG268 |
A | ASP296 |
A | SER297 |
A | GLY298 |
A | ARG300 |
A | GLY319 |
A | ALA92 |
A | ARG320 |
A | HOH386 |
A | HOH406 |
A | HOH430 |
A | PRO93 |
A | ILE94 |
A | ALA95 |
A | SER122 |
A | GLN144 |
A | TYR146 |
A | THR172 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 376 |
Chain | Residue |
A | TYR146 |
A | ASP174 |
A | THR176 |
A | HIS265 |
A | GLN269 |
A | HOH492 |
site_id | AC3 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FMN B 375 |
Chain | Residue |
B | ILE41 |
B | ALA92 |
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 | ARG300 |
B | GLY319 |
B | ARG320 |
B | HOH400 |
B | HOH478 |
B | HOH483 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 376 |
Chain | Residue |
B | TYR146 |
B | THR172 |
B | ASP174 |
B | THR176 |
B | HIS265 |
B | GLN269 |
B | HOH540 |
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 | |
Chain | Residue | Details |
A | TYR40 | |
B | TYR215 | |
B | HIS265 | |
B | ARG268 | |
A | TYR146 | |
A | ARG181 | |
A | TYR215 | |
A | HIS265 | |
A | ARG268 | |
B | TYR40 | |
B | TYR146 | |
B | ARG181 | |
Chain | Residue | Details |
A | PRO93 | |
A | ASP296 | |
A | ARG320 | |
B | PRO93 | |
B | ASP296 | |
B | ARG320 | |
Chain | Residue | Details |
A | SER122 | |
A | THR172 | |
A | LYS241 | |
A | SER263 | |
B | SER122 | |
B | THR172 | |
B | LYS241 | |
B | SER263 | |
Chain | Residue | Details |
A | GLN144 | |
B | GLN144 | |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
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 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
A | TYR40 | |
A | ARG268 | |
A | ASP174 | |
A | HIS265 | |
A | TYR146 | |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
B | TYR40 | |
B | ARG268 | |
B | ASP174 | |
B | HIS265 | |
B | TYR146 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
A | ARG268 | |
A | HIS265 | |
A | ASP174 | |
A | TYR146 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1fcb |
Chain | Residue | Details |
B | ARG268 | |
B | HIS265 | |
B | ASP174 | |
B | TYR146 | |