1DRA
CRYSTAL STRUCTURE OF UNLIGANDED ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. LIGAND-INDUCED CONFORMATIONAL CHANGES AND COOPERATIVITY IN BINDING
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 |
B | 0004146 | molecular_function | dihydrofolate reductase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005542 | molecular_function | folic acid binding |
B | 0005829 | cellular_component | cytosol |
B | 0006730 | biological_process | one-carbon metabolic process |
B | 0009257 | biological_process | 10-formyltetrahydrofolate biosynthetic process |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0031427 | biological_process | response to methotrexate |
B | 0046452 | biological_process | dihydrofolate metabolic process |
B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
B | 0046655 | biological_process | folic acid metabolic process |
B | 0046656 | biological_process | folic acid biosynthetic process |
B | 0046677 | biological_process | response to antibiotic |
B | 0050661 | molecular_function | NADP binding |
B | 0051870 | molecular_function | methotrexate binding |
B | 0051871 | molecular_function | dihydrofolic acid binding |
B | 0070401 | molecular_function | NADP+ binding |
B | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
site_id | AAB |
Number of Residues | 5 |
Details |
Chain | Residue |
A | LEU28 |
A | PHE31 |
A | ILE50 |
A | ARG52 |
A | LEU54 |
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 401 |
Chain | Residue |
A | GLY43 |
A | HIS45 |
A | THR46 |
A | GLY96 |
A | HOH613 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 605 |
Chain | Residue |
B | GLY43 |
B | HIS45 |
B | THR46 |
B | GLY96 |
B | HOH748 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 620 |
Chain | Residue |
A | HOH489 |
B | SER135 |
B | HOH664 |
B | HOH665 |
B | HOH667 |
B | HOH680 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE MTX A 161 |
Chain | Residue |
A | ILE5 |
A | ALA6 |
A | GLU27 |
A | PHE31 |
A | LYS32 |
A | SER49 |
A | ILE50 |
A | ARG52 |
A | ARG57 |
A | ILE94 |
A | TYR100 |
A | THR113 |
A | HOH405 |
A | HOH502 |
A | HOH535 |
A | HOH538 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE MTX B 361 |
Chain | Residue |
B | ILE5 |
B | ALA6 |
B | GLU27 |
B | PHE31 |
B | LYS32 |
B | ILE50 |
B | ARG52 |
B | ARG57 |
B | ILE94 |
B | TYR100 |
B | HOH661 |
B | HOH722 |
B | HOH787 |
site_id | AGL |
Number of Residues | 5 |
Details |
Chain | Residue |
A | LEU28 |
A | PHE31 |
A | LYS32 |
A | LEU54 |
A | ARG57 |
site_id | ANM |
Number of Residues | 1 |
Details |
Chain | Residue |
A | SER49 |
site_id | APT |
Number of Residues | 12 |
Details |
Chain | Residue |
A | ILE5 |
A | HOH403 |
A | HOH405 |
A | HOH411 |
A | ALA6 |
A | ALA7 |
A | TRP22 |
A | GLU27 |
A | LEU28 |
A | PHE31 |
A | ILE94 |
A | THR113 |
site_id | BAB |
Number of Residues | 5 |
Details |
Chain | Residue |
B | LEU28 |
B | PHE31 |
B | ILE50 |
B | ARG52 |
B | LEU54 |
site_id | BGL |
Number of Residues | 5 |
Details |
Chain | Residue |
B | LEU28 |
B | PHE31 |
B | LYS32 |
B | LEU54 |
B | ARG57 |
site_id | BNM |
Number of Residues | 1 |
Details |
Chain | Residue |
B | SER49 |
site_id | BPT |
Number of Residues | 12 |
Details |
Chain | Residue |
B | ILE5 |
B | ALA6 |
B | ALA7 |
B | TRP22 |
B | GLU27 |
B | LEU28 |
B | PHE31 |
B | ILE94 |
B | THR113 |
B | HOH628 |
B | HOH629 |
B | HOH661 |
Functional Information from PROSITE/UniProt
site_id | PS00075 |
Number of Residues | 23 |
Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGmenaMPWnlpa.ElawFkrnT |
Chain | Residue | Details |
A | VAL13-THR35 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9012674 |
Chain | Residue | Details |
A | ILE5 | |
B | THR113 | |
A | GLU27 | |
A | ARG52 | |
A | ARG57 | |
A | THR113 | |
B | ILE5 | |
B | GLU27 | |
B | ARG52 | |
B | ARG57 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19374017 |
Chain | Residue | Details |
A | ALA7 | |
B | SER63 | |
B | LYS76 | |
B | GLY95 | |
A | VAL13 | |
A | HIS45 | |
A | SER63 | |
A | LYS76 | |
A | GLY95 | |
B | ALA7 | |
B | VAL13 | |
B | HIS45 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1ra2 |
Chain | Residue | Details |
A | LEU54 | |
A | LEU28 | |
A | PHE31 | |
A | GLU27 | |
A | ILE5 | |
A | MET20 | |
A | ILE94 |
site_id | CSA2 |
Number of Residues | 7 |
Details | Annotated By Reference To The Literature 1ra2 |
Chain | Residue | Details |
B | LEU54 | |
B | LEU28 | |
B | PHE31 | |
B | GLU27 | |
B | ILE5 | |
B | MET20 | |
B | ILE94 |