6ITK
Crystal structure of malate dehydrogenase from Corynebacterium glutamicum ATCC 13032 in complex with NAD and malate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016615 | molecular_function | malate dehydrogenase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016615 | molecular_function | malate dehydrogenase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue LMR A 500 |
| Chain | Residue |
| A | ASN136 |
| A | ARG167 |
| A | HIS192 |
| A | GLY231 |
| A | SER242 |
| A | NAD501 |
| A | HOH609 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | GLN20 |
| A | ILE21 |
| A | GLU47 |
| A | ILE48 |
| A | VAL92 |
| A | GLY93 |
| A | ALA94 |
| A | ILE113 |
| A | GLN117 |
| A | VAL134 |
| A | GLY135 |
| A | ASN136 |
| A | MET160 |
| A | HIS192 |
| A | LMR500 |
| A | HOH611 |
| A | HOH614 |
| A | HOH645 |
| A | HOH649 |
| A | HOH653 |
| A | HOH676 |
| A | GLY16 |
| A | GLY19 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue LMR B 500 |
| Chain | Residue |
| B | ASN136 |
| B | ARG167 |
| B | HIS192 |
| B | GLY231 |
| B | SER242 |
| B | NAD501 |
| B | HOH642 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| B | GLY16 |
| B | GLY19 |
| B | GLN20 |
| B | ILE21 |
| B | GLU47 |
| B | ILE48 |
| B | VAL92 |
| B | GLY93 |
| B | ALA94 |
| B | PRO96 |
| B | ILE113 |
| B | GLN117 |
| B | VAL134 |
| B | GLY135 |
| B | ASN136 |
| B | MET160 |
| B | HIS192 |
| B | ALA246 |
| B | LMR500 |
| B | HOH607 |
| B | HOH626 |
| B | HOH647 |
| B | HOH660 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01517","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01517","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
