7F22
L-lactate oxidase with pyruvate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
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 | |
| A | SER631-GLN637 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:27302031 |
| Chain | Residue | Details |
| A | HIS633 | |
| B | HIS633 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77, ECO:0007744|PDB:4RJE |
| Chain | Residue | Details |
| A | TYR408 | |
| B | TYR583 | |
| B | HIS633 | |
| B | ARG636 | |
| A | TYR514 | |
| A | ARG549 | |
| A | TYR583 | |
| A | HIS633 | |
| A | ARG636 | |
| B | TYR408 | |
| B | TYR514 | |
| B | ARG549 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2DU2, ECO:0007744|PDB:2E77, ECO:0007744|PDB:2NLI |
| Chain | Residue | Details |
| A | PRO461 | |
| A | ASP664 | |
| A | ARG688 | |
| B | PRO461 | |
| B | ASP664 | |
| B | ARG688 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2E77, ECO:0007744|PDB:2NLI |
| Chain | Residue | Details |
| A | SER490 | |
| A | THR540 | |
| A | LYS609 | |
| A | SER631 | |
| B | SER490 | |
| B | THR540 | |
| B | LYS609 | |
| B | SER631 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17517371, ECO:0007744|PDB:2E77 |
| Chain | Residue | Details |
| A | GLN512 | |
| B | GLN512 |
| 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 | TYR583 | |
| B | TYR583 |
