3JVX
Crystal structure of Bacillus anthracis dihydrofolate reductase complexed with NADPH and 2,4-diamino-5-(3-(3,4,5-trimethoxyphenyl)prop-1-ynyl)-6-ethylpyrimidine (UCP120A)
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 | 31 |
| Details | BINDING SITE FOR RESIDUE NDP A 207 |
| Chain | Residue |
| A | VAL7 |
| A | ARG45 |
| A | LYS46 |
| A | LYS46 |
| A | ASN47 |
| A | VAL63 |
| A | THR64 |
| A | ARG65 |
| A | HIS78 |
| A | PHE96 |
| A | GLY97 |
| A | ALA8 |
| A | GLY98 |
| A | ALA99 |
| A | GLN100 |
| A | ILE101 |
| A | HOH163 |
| A | HOH164 |
| A | EKB208 |
| A | HOH234 |
| A | HOH256 |
| A | HOH271 |
| A | ILE15 |
| A | HOH282 |
| A | HOH285 |
| A | GLY16 |
| A | ASN19 |
| A | ASN20 |
| A | LEU21 |
| A | TRP23 |
| A | GLY44 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE EKB A 208 |
| Chain | Residue |
| A | MET6 |
| A | VAL7 |
| A | ALA8 |
| A | ASN20 |
| A | LEU21 |
| A | TRP23 |
| A | GLU28 |
| A | VAL32 |
| A | ASN47 |
| A | ILE51 |
| A | PHE96 |
| A | TYR102 |
| A | THR115 |
| A | NDP207 |
| site_id | AC3 |
| Number of Residues | 34 |
| 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 | TRP23 |
| 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 | TYR102 |
| B | LEU104 |
| B | HOH166 |
| B | HOH168 |
| B | HOH191 |
| B | HOH197 |
| B | EKB208 |
| B | HOH209 |
| B | HOH220 |
| B | HOH221 |
| B | HOH237 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE EKB B 208 |
| Chain | Residue |
| B | MET6 |
| B | VAL7 |
| B | ALA8 |
| B | ASN20 |
| B | LEU21 |
| B | GLU28 |
| B | VAL32 |
| B | ASN47 |
| B | ILE51 |
| B | PHE96 |
| B | TYR102 |
| B | THR115 |
| 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 |
