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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517 |
Chain | Residue | Details |
A | HIS192 | |
B | HIS192 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517 |
Chain | Residue | Details |
A | GLY16 | |
B | ARG97 | |
B | ARG103 | |
B | ASN110 | |
B | GLN117 | |
B | VAL134 | |
B | ASN136 | |
B | ARG167 | |
A | ARG97 | |
A | ARG103 | |
A | ASN110 | |
A | GLN117 | |
A | VAL134 | |
A | ASN136 | |
A | ARG167 | |
B | GLY16 |