3GYF
Human DHFR with Z-isomer in Orthorhombic lattice
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 | 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 | 0051000 | biological_process | positive regulation of nitric-oxide synthase activity |
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 | 14 |
Details | BINDING SITE FOR RESIDUE 51P A 187 |
Chain | Residue |
A | ILE7 |
A | VAL115 |
A | TYR121 |
A | THR136 |
A | NDP188 |
A | HOH215 |
A | VAL8 |
A | ALA9 |
A | GLU30 |
A | PHE31 |
A | PHE34 |
A | THR56 |
A | SER59 |
A | ILE60 |
site_id | AC2 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NDP A 188 |
Chain | Residue |
A | VAL8 |
A | ALA9 |
A | ILE16 |
A | GLY17 |
A | LYS18 |
A | GLY20 |
A | ASP21 |
A | LEU22 |
A | GLY53 |
A | LYS54 |
A | LYS55 |
A | THR56 |
A | SER59 |
A | LEU75 |
A | SER76 |
A | ARG77 |
A | GLU78 |
A | ARG91 |
A | VAL115 |
A | GLY116 |
A | GLY117 |
A | SER118 |
A | SER119 |
A | VAL120 |
A | TYR121 |
A | THR146 |
A | 51P187 |
A | HOH208 |
A | HOH215 |
A | HOH232 |
A | HOH255 |
A | HOH286 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 189 |
Chain | Residue |
A | ARG28 |
A | LYS68 |
A | GLY69 |
A | HOH229 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 190 |
Chain | Residue |
A | PRO66 |
A | ILE71 |
A | ASN72 |
A | HIS87 |
A | LEU153 |
A | GLU154 |
A | HOH199 |
A | HOH250 |
A | HOH254 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 191 |
Chain | Residue |
A | ASN13 |
A | PRO163 |
A | GLY164 |
A | HOH226 |
A | HOH276 |
Functional Information from PROSITE/UniProt
site_id | PS00075 |
Number of Residues | 24 |
Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkngdLPWpplrnEfryFqrmT |
Chain | Residue | Details |
A | GLY15-THR38 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15039552, ECO:0000269|PubMed:16222560, ECO:0000269|PubMed:19478082 |
Chain | Residue | Details |
A | ALA9 | |
A | GLY15 | |
A | LYS54 | |
A | SER76 | |
A | GLY116 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:2248959 |
Chain | Residue | Details |
A | GLU30 | |
A | ASN64 | |
A | ARG70 |
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 |