3QL3
Re-refined coordinates for PDB entry 1RX2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005542 | molecular_function | folic acid binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0009257 | biological_process | 10-formyltetrahydrofolate biosynthetic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0031427 | biological_process | response to methotrexate |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046452 | biological_process | dihydrofolate metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0046656 | biological_process | folic acid biosynthetic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051870 | molecular_function | methotrexate binding |
| A | 0051871 | molecular_function | dihydrofolic acid binding |
| A | 0070401 | molecular_function | NADP+ binding |
| A | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FOL A 161 |
| Chain | Residue |
| A | ILE5 |
| A | ARG57 |
| A | ILE94 |
| A | THR113 |
| A | NAP160 |
| A | HOH164 |
| A | HOH192 |
| A | HOH201 |
| A | HOH209 |
| A | HOH236 |
| A | ALA6 |
| A | ALA7 |
| A | MET20 |
| A | ASP27 |
| A | PHE31 |
| A | LYS32 |
| A | ILE50 |
| A | ARG52 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAP A 160 |
| Chain | Residue |
| A | ALA6 |
| A | ALA7 |
| A | ILE14 |
| A | GLY15 |
| A | MET16 |
| A | ASN18 |
| A | ALA19 |
| A | MET20 |
| A | GLY43 |
| A | ARG44 |
| A | HIS45 |
| A | THR46 |
| A | SER49 |
| A | LEU62 |
| A | SER63 |
| A | SER64 |
| A | LYS76 |
| A | ILE94 |
| A | GLY96 |
| A | GLY97 |
| A | ARG98 |
| A | VAL99 |
| A | TYR100 |
| A | GLN102 |
| A | ASP131 |
| A | FOL161 |
| A | HOH171 |
| A | HOH186 |
| A | HOH201 |
| A | HOH228 |
| A | HOH229 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 162 |
| Chain | Residue |
| A | ASP116 |
| A | HIS149 |
| A | ARG159 |
| A | HOH166 |
| A | HOH184 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 163 |
| Chain | Residue |
| A | ASP70 |
| A | ASP87 |
| A | HOH235 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.DlawFkrnT |
| Chain | Residue | Details |
| A | VAL13-THR35 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 157 |
| Details | Domain: {"description":"DHFR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00660","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9012674","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 17 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19374017","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
