3F8Y
Correlations of Human Dihydrofolate Reductase with Structural Data for Human Active Site Mutant Enzyme Complexes
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000900 | molecular_function | mRNA regulatory element binding translation repressor activity |
A | 0003723 | molecular_function | RNA binding |
A | 0003729 | molecular_function | mRNA binding |
A | 0004146 | molecular_function | dihydrofolate reductase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005542 | molecular_function | folic acid binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005829 | cellular_component | cytosol |
A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
A | 0006730 | biological_process | one-carbon metabolic process |
A | 0008144 | molecular_function | obsolete drug binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0017148 | biological_process | negative regulation of translation |
A | 0031103 | biological_process | axon regeneration |
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 |
A | 0070402 | molecular_function | NADPH binding |
A | 1990825 | molecular_function | sequence-specific mRNA binding |
A | 2000121 | biological_process | regulation of removal of superoxide radicals |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE DH1 A 187 |
Chain | Residue |
A | ILE7 |
A | VAL115 |
A | THR136 |
A | NDP188 |
A | HOH309 |
A | VAL8 |
A | ALA9 |
A | GLU30 |
A | PHE31 |
A | PHE34 |
A | LYS35 |
A | THR56 |
A | ARG70 |
site_id | AC2 |
Number of Residues | 40 |
Details | BINDING SITE FOR RESIDUE NDP A 188 |
Chain | Residue |
A | VAL8 |
A | ALA9 |
A | ILE16 |
A | GLY20 |
A | LEU22 |
A | GLY53 |
A | LYS54 |
A | LYS55 |
A | THR56 |
A | SER59 |
A | LEU75 |
A | SER76 |
A | ARG77 |
A | GLU78 |
A | ARG91 |
A | SER92 |
A | VAL115 |
A | GLY116 |
A | GLY117 |
A | SER118 |
A | SER119 |
A | VAL120 |
A | TYR121 |
A | THR146 |
A | DH1187 |
A | HOH195 |
A | HOH261 |
A | HOH353 |
A | HOH397 |
A | HOH404 |
A | HOH406 |
A | HOH437 |
A | HOH456 |
A | HOH457 |
A | HOH465 |
A | HOH485 |
A | HOH499 |
A | HOH511 |
A | HOH529 |
A | HOH549 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 189 |
Chain | Residue |
A | PRO149 |
A | GLU150 |
A | HOH301 |
A | HOH349 |
A | HOH351 |
A | HOH462 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 190 |
Chain | Residue |
A | GLU143 |
A | VAL165 |
A | LEU166 |
A | SER167 |
A | HOH200 |
A | HOH225 |
A | HOH341 |
A | HOH345 |
Functional Information from PROSITE/UniProt
site_id | PS00075 |
Number of Residues | 24 |
Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkngdLPWpplrnEfryFkrmT |
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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15039552","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16222560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19478082","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"2248959","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
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 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 490 |
Chain | Residue | Details |
A | LEU22 | electrostatic stabiliser |
A | GLU30 | electrostatic stabiliser |