9QCG
Crystal structure of Methanopyrus kandleri malate dehydrogenase mutant 4 at room temperature
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| A | 0006089 | biological_process | lactate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| A | 0046554 | molecular_function | L-malate dehydrogenase (NADP+) activity |
| B | 0004459 | molecular_function | L-lactate dehydrogenase (NAD+) activity |
| B | 0006089 | biological_process | lactate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| B | 0046554 | molecular_function | L-malate dehydrogenase (NADP+) activity |
Functional Information from PROSITE/UniProt
| site_id | PS00064 |
| Number of Residues | 7 |
| Details | L_LDH L-lactate dehydrogenase active site. IGEHGDT |
| Chain | Residue | Details |
| A | ILE175-THR181 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q60176","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P61889","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
