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 | |
