Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FOL A 201 |
| Chain | Residue |
| A | ILE5 |
| A | ARG53 |
| A | ARG58 |
| A | ILE95 |
| A | THR114 |
| A | NAP202 |
| A | HOH301 |
| A | HOH340 |
| A | HOH349 |
| A | HOH372 |
| A | HOH429 |
| A | ALA6 |
| A | HOH466 |
| A | ALA7 |
| A | MET20 |
| A | ASP28 |
| A | LEU29 |
| A | PHE32 |
| A | LYS33 |
| A | ILE51 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE NAP A 202 |
| Chain | Residue |
| A | ALA6 |
| A | ALA7 |
| A | ILE14 |
| A | GLY15 |
| A | ASN18 |
| A | ALA19 |
| A | MET20 |
| A | TRP22 |
| A | GLY44 |
| A | ARG45 |
| A | HIS46 |
| A | THR47 |
| A | SER50 |
| A | LEU63 |
| A | SER64 |
| A | SER65 |
| A | GLN66 |
| A | LYS77 |
| A | VAL79 |
| A | ILE95 |
| A | GLY96 |
| A | GLY97 |
| A | GLY98 |
| A | ARG99 |
| A | VAL100 |
| A | TYR101 |
| A | GLN103 |
| A | THR124 |
| A | ASP132 |
| A | FOL201 |
| A | HOH303 |
| A | HOH306 |
| A | HOH317 |
| A | HOH322 |
| A | HOH347 |
| A | HOH348 |
| A | HOH349 |
| A | HOH350 |
| A | HOH369 |
| A | HOH454 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 24 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWpplpaDlawFkrnT |
| Chain | Residue | Details |
| A | VAL13-THR36 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9012674","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 17 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19374017","evidenceCode":"ECO:0000269"}]} |
