4M1Q
Crystal structure of L-lactate dehydrogenase from Bacillus selenitireducens MLS10, NYSGRC Target 029814.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | ARG155 |
| B | SER192 |
| B | HOH508 |
| A | HIS170 |
| A | TYR172 |
| A | HOH505 |
| A | HOH520 |
| A | HOH539 |
| B | ASN168 |
| B | HIS170 |
| B | GLY191 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 402 |
| Chain | Residue |
| A | MSE48 |
| A | ASN51 |
| A | HIS52 |
| A | HOH603 |
| B | PHE156 |
| B | ASN217 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD A 403 |
| Chain | Residue |
| A | ASP212 |
| B | ASP266 |
| B | ASP268 |
| B | HOH749 |
| B | HOH750 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD A 404 |
| Chain | Residue |
| A | GLY81 |
| A | ILE100 |
| A | HOH536 |
| A | HOH630 |
| A | HOH777 |
| B | PRO312 |
| B | PHE314 |
| B | HOH681 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 B 401 |
| Chain | Residue |
| A | ASN168 |
| A | HIS170 |
| A | GLY191 |
| A | SER192 |
| B | ARG155 |
| B | HIS170 |
| B | TYR172 |
| B | HOH506 |
| B | HOH511 |
| B | HOH513 |
| B | HOH589 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 402 |
| Chain | Residue |
| A | PHE156 |
| A | ASN217 |
| B | MSE48 |
| B | ASN51 |
| B | HIS52 |
| B | HOH565 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD B 403 |
| Chain | Residue |
| A | LEU38 |
| A | ASP39 |
| B | ALA98 |
| B | ASN99 |
| B | LYS102 |
| B | HOH777 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MPD B 404 |
| Chain | Residue |
| B | TRP185 |
| B | ASN208 |
| B | ASP212 |
| B | HOH595 |
| B | HOH675 |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. MGEHGDT |
| Chain | Residue | Details |
| A | MSE174-THR180 |
