3F8Z
Human Dihydrofolate Reductase Structural Data with Active Site Mutant Enzyme Complexes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000900 | molecular_function | mRNA regulatory element binding translation repressor activity |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005542 | molecular_function | folic acid binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008144 | molecular_function | obsolete drug binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0017148 | biological_process | negative regulation of translation |
| A | 0031103 | biological_process | axon regeneration |
| A | 0031427 | biological_process | response to methotrexate |
| A | 0046452 | biological_process | dihydrofolate metabolic process |
| A | 0046653 | biological_process | tetrahydrofolate metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051000 | biological_process | positive regulation of nitric-oxide synthase activity |
| A | 0070402 | molecular_function | NADPH binding |
| A | 1990825 | molecular_function | sequence-specific mRNA binding |
| A | 2000121 | biological_process | regulation of removal of superoxide radicals |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DH1 A 187 |
| Chain | Residue |
| A | ILE7 |
| A | VAL115 |
| A | THR136 |
| A | NDP188 |
| A | HOH237 |
| A | HOH356 |
| A | VAL8 |
| A | ALA9 |
| A | GLU30 |
| A | PHE34 |
| A | SER35 |
| A | THR56 |
| A | LEU67 |
| A | ARG70 |
| site_id | AC2 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NDP A 188 |
| Chain | Residue |
| A | VAL8 |
| A | ALA9 |
| A | ILE16 |
| A | GLY20 |
| A | ASP21 |
| A | LEU22 |
| A | GLY53 |
| A | LYS54 |
| A | LYS55 |
| A | THR56 |
| A | SER59 |
| A | LEU75 |
| A | SER76 |
| A | ARG77 |
| A | GLU78 |
| A | ARG91 |
| A | SER92 |
| A | VAL115 |
| A | GLY117 |
| A | SER118 |
| A | SER119 |
| A | VAL120 |
| A | TYR121 |
| A | DH1187 |
| A | HOH206 |
| A | HOH228 |
| A | HOH258 |
| A | HOH325 |
| A | HOH332 |
| A | HOH364 |
| A | HOH378 |
| A | HOH381 |
| A | HOH407 |
| A | HOH455 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 189 |
| Chain | Residue |
| A | ASN19 |
| A | LEU158 |
| A | LEU159 |
| A | PRO160 |
| A | GLU161 |
| A | TYR162 |
| A | PHE179 |
| A | GLU180 |
| A | VAL181 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 190 |
| Chain | Residue |
| A | LYS122 |
| A | PRO149 |
| A | GLU150 |
| A | HOH374 |
| A | HOH392 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 191 |
| Chain | Residue |
| A | GLU172 |
| A | LYS173 |
| A | HOH366 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 192 |
| Chain | Residue |
| A | ASN13 |
| A | PHE147 |
| A | HOH262 |
| A | HOH276 |
| A | HOH418 |
| A | HOH442 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 193 |
| Chain | Residue |
| A | PRO25 |
| A | LYS68 |
| A | LYS173 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 24 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkngdLPWpplrnEfryFsrmT |
| Chain | Residue | Details |
| A | GLY15-THR38 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082 |
| Chain | Residue | Details |
| A | ALA9 | |
| A | GLY15 | |
| A | LYS54 | |
| A | SER76 | |
| A | GLY116 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:2248959 |
| Chain | Residue | Details |
| A | GLU30 | |
| A | SER64 | |
| A | ARG70 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| A | LEU22 | |
| A | GLU30 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 490 |
| Chain | Residue | Details |
| A | LEU22 | electrostatic stabiliser |
| A | GLU30 | electrostatic stabiliser |
