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 | 0006734 | biological_process | NADH 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 | 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 | 0006734 | biological_process | NADH 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 | 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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517 |
Chain | Residue | Details |
A | HIS189 | |
B | HIS189 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517 |
Chain | Residue | Details |
A | GLY13 | |
B | ARG94 | |
B | ARG100 | |
B | ASN107 | |
B | GLN114 | |
B | THR131 | |
B | ASN133 | |
B | ARG164 | |
A | ARG94 | |
A | ARG100 | |
A | ASN107 | |
A | GLN114 | |
A | THR131 | |
A | ASN133 | |
A | ARG164 | |
B | GLY13 |