3GHV
Human dihydrofolate reductase Q35K/N64F double mutant inhibitor complex
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 | 21 |
| Details | BINDING SITE FOR RESIDUE GHC A 187 |
| Chain | Residue |
| A | VAL8 |
| A | ARG70 |
| A | VAL115 |
| A | THR136 |
| A | NDP188 |
| A | HOH280 |
| A | HOH319 |
| A | HOH383 |
| A | HOH396 |
| A | HOH437 |
| A | HOH478 |
| A | ALA9 |
| A | HOH521 |
| A | HOH542 |
| A | LEU22 |
| A | GLU30 |
| A | PHE31 |
| A | PHE34 |
| A | LYS35 |
| A | THR56 |
| A | PHE64 |
| site_id | AC2 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE NDP A 188 |
| Chain | Residue |
| A | VAL8 |
| A | ALA9 |
| A | ILE16 |
| A | GLY17 |
| A | GLY20 |
| A | ASP21 |
| A | LEU22 |
| A | GLY53 |
| A | LYS54 |
| A | LYS55 |
| A | THR56 |
| A | LEU75 |
| A | SER76 |
| A | ARG77 |
| A | GLU78 |
| A | ARG91 |
| A | SER92 |
| A | VAL115 |
| A | GLY117 |
| A | SER118 |
| A | TYR121 |
| A | THR146 |
| A | GHC187 |
| A | HOH230 |
| A | HOH255 |
| A | HOH288 |
| A | HOH370 |
| A | HOH387 |
| A | HOH409 |
| A | HOH412 |
| A | HOH461 |
| A | HOH498 |
| A | HOH500 |
| A | HOH528 |
| A | HOH537 |
| A | HOH548 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 189 |
| Chain | Residue |
| A | PRO61 |
| A | GLU62 |
| A | LYS157 |
| A | HOH201 |
| A | HOH290 |
| A | HOH425 |
| A | HOH456 |
| A | HOH504 |
| A | HOH527 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 190 |
| Chain | Residue |
| A | LYS63 |
| A | LYS63 |
| A | PHE64 |
| A | HOH285 |
| A | HOH285 |
| A | HOH285 |
| A | HOH330 |
| A | HOH330 |
| A | HOH335 |
| A | HOH521 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 191 |
| Chain | Residue |
| A | LYS122 |
| A | PRO149 |
| A | GLU150 |
| A | HOH360 |
| A | HOH438 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 192 |
| Chain | Residue |
| A | ASN19 |
| A | LEU158 |
| A | LEU159 |
| A | PRO160 |
| A | GLU161 |
| A | TYR162 |
| A | VAL165 |
| A | PHE179 |
| A | GLU180 |
| A | VAL181 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 193 |
| Chain | Residue |
| A | HOH323 |
| A | PRO25 |
| A | PRO26 |
| A | LYS35 |
| A | LYS68 |
| A | LYS173 |
| A | HOH208 |
| A | HOH305 |
| A | HOH316 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 194 |
| Chain | Residue |
| A | LEU22 |
| A | PRO23 |
| A | TRP24 |
| A | LYS68 |
| A | HOH337 |
| A | HOH364 |
| A | HOH402 |
| A | HOH415 |
| A | HOH419 |
| A | HOH497 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 195 |
| Chain | Residue |
| A | GLU143 |
| A | LEU166 |
| A | SER167 |
| A | HOH239 |
| A | HOH277 |
| A | HOH459 |
| A | HOH530 |
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 |
