3JWK
Crystal structure of Bacillus anthracis (Y102F) dihydrofolate reductase complexed with NADPH and (S)-2,4-diamino-5-(3-methoxy-3-(3,4,5-trimethoxyphenyl)prop-1-ynyl)-6-methylpyrimidine (UCP114A)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004146 | molecular_function | dihydrofolate reductase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046452 | biological_process | dihydrofolate metabolic process |
| A | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004146 | molecular_function | dihydrofolate reductase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046452 | biological_process | dihydrofolate metabolic process |
| B | 0046654 | biological_process | tetrahydrofolate biosynthetic process |
| B | 0046655 | biological_process | folic acid metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NDP A 207 |
| Chain | Residue |
| A | VAL7 |
| A | LYS46 |
| A | LYS46 |
| A | ASN47 |
| A | VAL63 |
| A | THR64 |
| A | ARG65 |
| A | HIS78 |
| A | PHE96 |
| A | GLY97 |
| A | GLY98 |
| A | ALA8 |
| A | ALA99 |
| A | GLN100 |
| A | ILE101 |
| A | LEU104 |
| A | HOH164 |
| A | HOH167 |
| A | HOH184 |
| A | 5WB208 |
| A | HOH213 |
| A | HOH220 |
| A | ILE15 |
| A | HOH235 |
| A | HOH248 |
| A | HOH254 |
| A | HOH316 |
| A | HOH348 |
| A | GLY16 |
| A | ASN19 |
| A | ASN20 |
| A | LEU21 |
| A | GLY44 |
| A | ARG45 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 5WB A 208 |
| Chain | Residue |
| A | MET6 |
| A | VAL7 |
| A | ALA8 |
| A | GLU28 |
| A | LEU29 |
| A | VAL32 |
| A | ASN47 |
| A | PHE96 |
| A | HOH203 |
| A | NDP207 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NDP B 207 |
| Chain | Residue |
| B | VAL7 |
| B | ALA8 |
| B | ILE15 |
| B | GLY16 |
| B | ASN19 |
| B | ASN20 |
| B | LEU21 |
| B | GLY44 |
| B | ARG45 |
| B | LYS46 |
| B | LYS46 |
| B | ASN47 |
| B | VAL63 |
| B | THR64 |
| B | ARG65 |
| B | HIS78 |
| B | PHE96 |
| B | GLY97 |
| B | GLY98 |
| B | ALA99 |
| B | GLN100 |
| B | ILE101 |
| B | LEU104 |
| B | HOH166 |
| B | HOH180 |
| B | HOH182 |
| B | HOH187 |
| B | HOH206 |
| B | 5WB208 |
| B | HOH211 |
| B | HOH212 |
| B | HOH229 |
| B | HOH295 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 5WB B 208 |
| Chain | Residue |
| B | MET6 |
| B | VAL7 |
| B | ALA8 |
| B | LEU21 |
| B | GLU28 |
| B | LEU29 |
| B | VAL32 |
| B | ASN47 |
| B | ALA50 |
| B | PHE96 |
| B | HOH183 |
| B | NDP207 |
Functional Information from PROSITE/UniProt
| site_id | PS00075 |
| Number of Residues | 23 |
| Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGkdnnLPWrlps.ElqyVkktT |
| Chain | Residue | Details |
| A | VAL14-THR36 |
