Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005739 | cellular_component | mitochondrion |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE FOL A 207 |
| Chain | Residue |
| A | ILE10 |
| A | ALA12 |
| A | GLU32 |
| A | ILE33 |
| A | PHE36 |
| A | LYS37 |
| A | PHE69 |
| A | ARG75 |
| A | ILE123 |
| A | TYR129 |
| A | HOH215 |
| A | HOH216 |
| site_id | S1 |
| Number of Residues | 11 |
| Details | THE BINDING ORIENTATION OF THE PTERIDINE RING OF FOL IN THIS STRUCTURE IS SIMILAR TO THAT OBSERVED IN HDHFR FA BINARY COMPLEXES. |
| Chain | Residue |
| A | ILE10 |
| A | TYR129 |
| A | THR144 |
| A | LEU25 |
| A | TRP27 |
| A | GLU32 |
| A | ILE33 |
| A | PHE36 |
| A | ILE65 |
| A | PRO66 |
| A | ILE123 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGrsnsLPWklkk.EisyFkrvT |
| Chain | Residue | Details |
| A | GLY18-THR40 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ALA12 | |
| A | GLY18 | |
| A | ARG59 | |
| A | THR81 | |
| A | GLY124 | |
| Chain | Residue | Details |
| A | GLU32 | |
| A | ARG75 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dhf |
| Chain | Residue | Details |
| A | LEU25 | |
| A | GLU32 | |
