8RWL
Crystal structure of Methanopyrus kandleri malate dehydrogenase mutant 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004459 | molecular_function | L-lactate dehydrogenase activity |
A | 0006089 | biological_process | lactate metabolic process |
A | 0006090 | biological_process | pyruvate 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 activity |
B | 0006089 | biological_process | lactate metabolic process |
B | 0006090 | biological_process | pyruvate 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 | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P61889 |
Chain | Residue | Details |
A | HIS178 | |
B | HIS178 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q60176 |
Chain | Residue | Details |
A | GLY8 | |
A | ASN98 | |
A | VAL121 | |
B | GLY8 | |
B | ASN98 | |
B | VAL121 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P61889 |
Chain | Residue | Details |
A | GLN85 | |
A | ARG91 | |
A | ASN123 | |
A | ARG154 | |
B | GLN85 | |
B | ARG91 | |
B | ASN123 | |
B | ARG154 |