4NX7
single cryogenic temperature model of DHFR
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 | 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 | 7 |
Details | BINDING SITE FOR RESIDUE MN A 201 |
Chain | Residue |
A | ASP116 |
A | HIS149 |
A | ARG159 |
A | HOH335 |
A | HOH350 |
A | HOH351 |
A | HOH553 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FOL A 202 |
Chain | Residue |
A | ALA7 |
A | MET20 |
A | ASP27 |
A | LEU28 |
A | PHE31 |
A | LYS32 |
A | ILE50 |
A | ARG57 |
A | ILE94 |
A | TYR100 |
A | THR113 |
A | NAP204 |
A | HOH301 |
A | HOH307 |
A | HOH324 |
A | HOH353 |
A | HOH433 |
A | HOH446 |
A | HOH491 |
A | HOH527 |
A | ILE5 |
A | ALA6 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BME A 203 |
Chain | Residue |
A | HIS114 |
A | SER138 |
A | CYS152 |
A | HOH474 |
A | HOH595 |
site_id | AC4 |
Number of Residues | 38 |
Details | BINDING SITE FOR RESIDUE NAP A 204 |
Chain | Residue |
A | ALA6 |
A | ALA7 |
A | ILE14 |
A | GLY15 |
A | ASN18 |
A | ALA19 |
A | MET20 |
A | TRP22 |
A | GLY43 |
A | ARG44 |
A | HIS45 |
A | THR46 |
A | LEU62 |
A | SER63 |
A | SER64 |
A | LYS76 |
A | ILE94 |
A | GLY96 |
A | GLY97 |
A | ARG98 |
A | VAL99 |
A | TYR100 |
A | GLN102 |
A | THR123 |
A | ASP131 |
A | FOL202 |
A | HOH307 |
A | HOH309 |
A | HOH316 |
A | HOH323 |
A | HOH349 |
A | HOH371 |
A | HOH381 |
A | HOH397 |
A | HOH415 |
A | HOH540 |
A | HOH550 |
A | HOH559 |
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 | 5 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9012674 |
Chain | Residue | Details |
A | ILE5 | |
A | ASP27 | |
A | ARG52 | |
A | ARG57 | |
A | THR113 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19374017 |
Chain | Residue | Details |
A | ALA7 | |
A | VAL13 | |
A | HIS45 | |
A | SER63 | |
A | LYS76 | |
A | GLY95 |