6NNI
Structure of closed state of Dihydrofolate reductase from Mycobacterium tuberculosis in complex with NADPH and pyrimethamine
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 | 6 |
Details | binding site for residue CO A 201 |
Chain | Residue |
A | HIS38 |
A | HOH334 |
A | HOH360 |
A | HOH382 |
B | HIS157 |
B | HOH392 |
site_id | AC2 |
Number of Residues | 32 |
Details | binding site for residue NDP A 202 |
Chain | Residue |
A | GLY15 |
A | ARG16 |
A | GLY18 |
A | ASP19 |
A | ILE20 |
A | GLY43 |
A | ARG44 |
A | ARG45 |
A | THR46 |
A | LEU65 |
A | SER66 |
A | ARG67 |
A | GLN68 |
A | GLY80 |
A | ILE94 |
A | GLY95 |
A | GLY96 |
A | GLY97 |
A | GLN98 |
A | VAL99 |
A | TYR100 |
A | CP6203 |
A | HOH326 |
A | HOH329 |
A | HOH341 |
A | HOH347 |
A | HOH352 |
A | HOH357 |
A | HOH396 |
A | TRP6 |
A | ALA7 |
A | ILE14 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue CP6 A 203 |
Chain | Residue |
A | ILE5 |
A | TRP6 |
A | ALA7 |
A | ASP27 |
A | GLN28 |
A | PHE31 |
A | THR46 |
A | LEU50 |
A | ILE94 |
A | TYR100 |
A | THR113 |
A | NDP202 |
A | MES204 |
A | HOH384 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue MES A 204 |
Chain | Residue |
A | GLN28 |
A | PHE31 |
A | ARG32 |
A | LEU57 |
A | ARG60 |
A | CP6203 |
A | HOH308 |
A | HOH420 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 205 |
Chain | Residue |
A | ARG136 |
B | GLU26 |
B | ALA29 |
B | ARG146 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 206 |
Chain | Residue |
A | PRO51 |
A | ALA52 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 207 |
Chain | Residue |
A | ARG44 |
A | ARG45 |
A | HOH312 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CO B 201 |
Chain | Residue |
A | HOH387 |
B | HIS38 |
B | HOH309 |
B | HOH310 |
B | HOH353 |
B | HOH355 |
site_id | AC9 |
Number of Residues | 34 |
Details | binding site for residue NDP B 202 |
Chain | Residue |
B | LEU102 |
B | ALA126 |
B | CP6203 |
B | HOH322 |
B | HOH329 |
B | HOH339 |
B | HOH345 |
B | HOH347 |
B | HOH358 |
B | HOH363 |
B | TRP6 |
B | ALA7 |
B | ILE14 |
B | GLY15 |
B | ARG16 |
B | GLY18 |
B | ASP19 |
B | ILE20 |
B | GLY43 |
B | ARG44 |
B | ARG45 |
B | THR46 |
B | LEU65 |
B | SER66 |
B | ARG67 |
B | GLN68 |
B | GLY80 |
B | ILE94 |
B | GLY95 |
B | GLY96 |
B | GLY97 |
B | GLN98 |
B | VAL99 |
B | TYR100 |
site_id | AD1 |
Number of Residues | 13 |
Details | binding site for residue CP6 B 203 |
Chain | Residue |
B | ILE5 |
B | TRP6 |
B | ALA7 |
B | ILE20 |
B | ASP27 |
B | PHE31 |
B | THR46 |
B | LEU50 |
B | ILE94 |
B | TYR100 |
B | NDP202 |
B | MES204 |
B | HOH373 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MES B 204 |
Chain | Residue |
B | GLN28 |
B | PHE31 |
B | ARG32 |
B | ARG60 |
B | CP6203 |
B | HOH303 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue SO4 B 205 |
Chain | Residue |
B | ARG44 |
B | ARG45 |
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 | ILE5 | |
A | ILE94 | |
A | TYR100 | |
A | THR113 | |
B | ILE5 | |
B | TRP6 | |
B | ILE14 | |
B | ASP27 | |
B | ARG32 | |
B | GLY43 | |
B | ARG60 | |
A | TRP6 | |
B | LEU65 | |
B | GLY80 | |
B | ILE94 | |
B | TYR100 | |
B | THR113 | |
A | ILE14 | |
A | ASP27 | |
A | ARG32 | |
A | GLY43 | |
A | ARG60 | |
A | LEU65 | |
A | GLY80 |