6NNC
Structure of Dihydrofolate reductase from Mycobacterium tuberculosis in complex with NADPH and pemetrexed
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 | 35 |
Details | binding site for residue NDP A 201 |
Chain | Residue |
A | TRP6 |
A | ARG44 |
A | ARG45 |
A | THR46 |
A | LEU65 |
A | SER66 |
A | ARG67 |
A | GLN68 |
A | GLY80 |
A | ILE94 |
A | GLY96 |
A | ALA7 |
A | GLY97 |
A | GLN98 |
A | VAL99 |
A | TYR100 |
A | LEU102 |
A | ALA126 |
A | LYA203 |
A | HOH306 |
A | HOH318 |
A | HOH325 |
A | ILE14 |
A | HOH337 |
A | HOH338 |
A | HOH351 |
A | HOH360 |
A | HOH379 |
A | HOH399 |
A | GLY15 |
A | ARG16 |
A | GLY18 |
A | ASP19 |
A | ILE20 |
A | GLY43 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CO A 202 |
Chain | Residue |
A | HIS38 |
A | HOH327 |
A | HOH345 |
A | HOH346 |
B | HIS157 |
B | HOH391 |
site_id | AC3 |
Number of Residues | 20 |
Details | binding site for residue LYA A 203 |
Chain | Residue |
A | ILE5 |
A | TRP6 |
A | ALA7 |
A | ASP27 |
A | GLN28 |
A | PHE31 |
A | ARG32 |
A | LEU50 |
A | LEU57 |
A | ARG60 |
A | ILE94 |
A | TYR100 |
A | THR113 |
A | NDP201 |
A | HOH324 |
A | HOH350 |
A | HOH362 |
A | HOH393 |
A | HOH401 |
A | HOH411 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 204 |
Chain | Residue |
A | ARG23 |
A | PRO51 |
A | HOH309 |
A | HOH367 |
B | ARG32 |
B | PRO58 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue SO4 A 205 |
Chain | Residue |
A | ARG44 |
A | ARG45 |
site_id | AC6 |
Number of Residues | 33 |
Details | binding site for residue NDP B 201 |
Chain | Residue |
B | HOH372 |
B | HOH382 |
B | HOH389 |
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 | GLY96 |
B | GLY97 |
B | GLN98 |
B | VAL99 |
B | TYR100 |
B | LEU102 |
B | LYA203 |
B | HOH321 |
B | HOH322 |
B | HOH331 |
B | HOH333 |
B | HOH358 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CO B 202 |
Chain | Residue |
A | HOH383 |
B | HIS38 |
B | HOH309 |
B | HOH335 |
B | HOH344 |
B | HOH395 |
site_id | AC8 |
Number of Residues | 21 |
Details | binding site for residue LYA B 203 |
Chain | Residue |
B | ILE5 |
B | TRP6 |
B | ALA7 |
B | ASP27 |
B | GLN28 |
B | ALA29 |
B | PHE31 |
B | ARG32 |
B | LEU50 |
B | VAL54 |
B | ARG60 |
B | ILE94 |
B | TYR100 |
B | NDP201 |
B | HOH304 |
B | HOH307 |
B | HOH310 |
B | HOH311 |
B | HOH355 |
B | HOH369 |
B | HOH371 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 204 |
Chain | Residue |
B | ARG44 |
B | ARG45 |
B | HOH394 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 205 |
Chain | Residue |
A | ARG136 |
A | HOH304 |
B | ALA29 |
B | ARG146 |
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 |