4I1I
Crystal structure of a putative Cytosolic malate dehydrogenase from Leishmania major Friedlin in complex with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| 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 | 0019674 | biological_process | NAD+ metabolic process |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030060 | molecular_function | L-malate dehydrogenase (NAD+) activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| 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 | 0019674 | biological_process | NAD+ metabolic process |
| 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 | 31 |
| Details | BINDING SITE FOR RESIDUE NAD A 400 |
| Chain | Residue |
| A | GLY10 |
| A | PHE89 |
| A | ILE107 |
| A | GLN111 |
| A | VAL128 |
| A | GLY129 |
| A | ASN130 |
| A | MET155 |
| A | HIS187 |
| A | SER237 |
| A | EDO404 |
| A | GLY13 |
| A | HOH514 |
| A | HOH534 |
| A | HOH545 |
| A | HOH605 |
| A | HOH623 |
| A | HOH625 |
| A | HOH632 |
| A | HOH641 |
| A | HOH667 |
| A | HOH697 |
| A | GLN14 |
| A | HOH726 |
| A | HOH727 |
| A | ILE15 |
| A | ASP41 |
| A | ILE42 |
| A | CYS86 |
| A | GLY87 |
| A | ALA88 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 401 |
| Chain | Residue |
| A | ARG25 |
| A | ALA27 |
| A | HOH525 |
| A | HOH613 |
| A | HOH647 |
| A | HOH749 |
| B | ARG25 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| A | LEU46 |
| A | ALA50 |
| A | VAL69 |
| A | HOH746 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | ASP269 |
| A | GLU270 |
| A | ASN271 |
| A | VAL275 |
| A | SER277 |
| A | HOH596 |
| B | ARG319 |
| B | LEU324 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | ASN130 |
| A | ARG162 |
| A | HIS187 |
| A | NAD400 |
| A | HOH564 |
| A | HOH650 |
| A | HOH740 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 405 |
| Chain | Residue |
| A | PRO193 |
| A | ASP194 |
| A | THR195 |
| A | ASP196 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 401 |
| Chain | Residue |
| B | GLY13 |
| B | GLN14 |
| B | HOH786 |
| B | HOH789 |
| B | HOH795 |
| B | HOH805 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 402 |
| Chain | Residue |
| B | ARG162 |
| B | GLY226 |
| B | SER237 |
| B | HOH529 |
| B | HOH634 |
| B | HOH649 |
| B | HOH754 |
| B | HOH806 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | PRO193 |
| B | ASP194 |
| B | THR195 |
| B | ASP196 |
| B | ARG307 |
Functional Information from PROSITE/UniProt
