4TVO
Structure of Malate Dehydrogenase from Mycobacterium tuberculosis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006099 | biological_process | tricarboxylic acid cycle |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0006108 | biological_process | malate metabolic process |
| A | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006099 | biological_process | tricarboxylic acid cycle |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| B | 0006108 | biological_process | malate metabolic process |
| B | 0009274 | cellular_component | peptidoglycan-based cell wall |
| 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 | 9 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | ARG94 |
| A | ARG100 |
| A | ARG164 |
| A | HIS189 |
| A | GLY229 |
| A | SER240 |
| A | HOH590 |
| A | HOH595 |
| A | HOH674 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | GLY29 |
| A | LEU32 |
| A | GLY33 |
| A | ARG36 |
| A | HOH569 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 403 |
| Chain | Residue |
| A | LEU160 |
| A | ASN163 |
| A | SER243 |
| A | ALA247 |
| B | ASP61 |
| B | CYS62 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 404 |
| Chain | Residue |
| A | MET143 |
| A | ALA146 |
| A | ILE149 |
| A | ARG151 |
| A | HOH640 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 405 |
| Chain | Residue |
| A | ALA315 |
| A | ASP319 |
| B | GLU304 |
| B | ARG307 |
| B | HOH506 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 406 |
| Chain | Residue |
| A | THR224 |
| A | LYS227 |
| A | ARG228 |
| A | ALA231 |
| A | NA407 |
| A | HOH672 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 407 |
| Chain | Residue |
| A | ARG228 |
| A | ALA231 |
| A | NA406 |
| A | HOH742 |
| A | HOH743 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 408 |
| Chain | Residue |
| A | GLN17 |
| A | SER21 |
| A | HOH638 |
| A | HOH693 |
| B | TYR20 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 409 |
| Chain | Residue |
| A | GLU71 |
| A | ILE72 |
| A | HOH669 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue NA A 410 |
| Chain | Residue |
| A | GLU218 |
| A | ARG309 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue NA A 411 |
| Chain | Residue |
| A | ARG228 |
| B | ASP60 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 412 |
| Chain | Residue |
| A | GLY16 |
| A | GLU44 |
| A | HOH646 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 413 |
| Chain | Residue |
| A | ARG94 |
| A | ARG100 |
| A | ALA226 |
| A | LYS227 |
| A | GLY229 |
| A | ALA230 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue NA A 414 |
| Chain | Residue |
| A | PRO278 |
| A | GLU279 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 415 |
| Chain | Residue |
| A | GLY280 |
| A | ARG321 |
| A | HOH735 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | ARG164 |
| B | GLY229 |
| B | SER240 |
| B | HOH636 |
| B | HOH637 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 402 |
| Chain | Residue |
| A | CYS62 |
| B | ASN163 |
| B | SER246 |
| B | ASP250 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 403 |
| Chain | Residue |
| A | ASP61 |
| A | CYS62 |
| B | LEU160 |
| B | ASN163 |
| B | SER243 |
| B | ALA247 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 404 |
| Chain | Residue |
| B | ARG151 |
| B | GLU152 |
| B | PHE154 |
| B | VAL270 |
| B | TRP294 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 405 |
| Chain | Residue |
| B | LEU26 |
| B | GLY29 |
| B | SER30 |
| B | LEU31 |
| B | LEU32 |
| B | HOH539 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 406 |
| Chain | Residue |
| B | THR295 |
| B | ILE296 |
| B | HOH727 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 407 |
| Chain | Residue |
| B | HOH661 |
| B | HOH728 |
| B | GLY13 |
| B | LEU43 |
| B | HOH619 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 408 |
| Chain | Residue |
| B | GLN17 |
| B | ILE18 |
| B | HOH656 |
| B | HOH688 |
| site_id | AE6 |
| Number of Residues | 8 |
| Details | binding site for residue NA B 409 |
| Chain | Residue |
| B | GLY129 |
| B | VAL130 |
| B | SER155 |
| B | ALA156 |
| B | LEU157 |
| B | HOH567 |
| B | HOH615 |
| B | HOH667 |
Functional Information from PROSITE/UniProt
| site_id | PS00068 |
| Number of Residues | 13 |
| Details | MDH Malate dehydrogenase active site signature. LTRLDhnRAisqL |
| Chain | Residue | Details |
| A | LEU157-LEU169 |
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 |
