Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008144 | molecular_function | obsolete drug binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE HG A 190 |
| Chain | Residue |
| A | CYS11 |
| A | ASN13 |
| A | GLY15 |
| A | GLU141 |
| A | PHE142 |
| A | SER144 |
| A | HOH705 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 200 |
| Chain | Residue |
| A | NAP191 |
| A | NAP191 |
| A | HOH278 |
| A | HOH278 |
| A | GLU78 |
| A | GLU78 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAP A 191 |
| Chain | Residue |
| A | VAL8 |
| A | ALA9 |
| A | ILE16 |
| A | GLY17 |
| A | GLY20 |
| A | ASN21 |
| A | LEU22 |
| A | GLY53 |
| A | LYS54 |
| A | LYS55 |
| A | THR56 |
| A | LEU75 |
| A | SER76 |
| A | ARG77 |
| A | GLU78 |
| A | GLU78 |
| A | LYS91 |
| A | SER92 |
| A | VAL115 |
| A | GLY117 |
| A | THR118 |
| A | ALA119 |
| A | VAL120 |
| A | TYR121 |
| A | HBI198 |
| A | CA200 |
| A | CA200 |
| A | HOH220 |
| A | HOH318 |
| A | HOH392 |
| A | HOH393 |
| A | HOH493 |
| A | HOH648 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HBI A 198 |
| Chain | Residue |
| A | ILE7 |
| A | VAL8 |
| A | ALA9 |
| A | LEU22 |
| A | GLU30 |
| A | PHE34 |
| A | VAL115 |
| A | THR136 |
| A | NAP191 |
| A | HOH230 |
| A | HOH648 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 24 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkdgnLPWpplrnEykyFqrmT |
| Chain | Residue | Details |
| A | GLY15-THR38 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 181 |
| Details | Domain: {"description":"DHFR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00660","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1510919","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DR1","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1510919","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00374","evidenceCode":"ECO:0000250"}]} |
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 | |
