4KLX
Crystal structure of dihydrofolate reductase from Mycobacterium tuberculosis in an open conformation.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046452 | biological_process | dihydrofolate metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070401 | molecular_function | NADP+ binding |
| B | 0004146 | molecular_function | dihydrofolate reductase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046452 | biological_process | dihydrofolate metabolic process |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046655 | biological_process | folic acid metabolic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 0070401 | molecular_function | NADP+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATR A 201 |
| Chain | Residue |
| A | GLY43 |
| A | GLY96 |
| A | GLY97 |
| A | GLN98 |
| A | VAL99 |
| A | LEU102 |
| A | HOH346 |
| A | HOH403 |
| A | HOH435 |
| A | HOH461 |
| A | HOH484 |
| A | ARG44 |
| A | HOH560 |
| A | ARG45 |
| A | THR46 |
| A | LEU65 |
| A | SER66 |
| A | ARG67 |
| A | GLN68 |
| A | GLY80 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ETE A 202 |
| Chain | Residue |
| A | GLU133 |
| A | ARG136 |
| A | HOH495 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATR B 200 |
| Chain | Residue |
| B | ARG32 |
| B | GLY43 |
| B | ARG44 |
| B | ARG45 |
| B | THR46 |
| B | LEU65 |
| B | SER66 |
| B | ARG67 |
| B | GLN68 |
| B | GLY80 |
| B | GLY96 |
| B | GLY97 |
| B | GLN98 |
| B | VAL99 |
| B | LEU102 |
| B | HOH326 |
| B | HOH396 |
| B | HOH437 |
| B | HOH475 |
| B | HOH490 |
| B | HOH526 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGrggdIPWrlpe.DqahFreiT |
| Chain | Residue | Details |
| A | VAL13-THR35 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU102 | |
| A | VAL115 | |
| B | ALA7 | |
| B | GLN8 | |
| B | ARG16 | |
| B | ALA29 | |
| B | ILE34 | |
| B | ARG45 | |
| B | ASN62 | |
| B | ARG67 | |
| B | LEU82 | |
| B | GLY96 | |
| B | LEU102 | |
| B | VAL115 | |
| A | ALA7 | |
| A | GLN8 | |
| A | ARG16 | |
| A | ALA29 | |
| A | ILE34 | |
| A | ARG45 | |
| A | ASN62 | |
| A | ARG67 | |
| A | LEU82 | |
| A | GLY96 |
