7KM8
Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium ulcerans Agy99 in complex with NADP and inhibitor SDDC-0001914, orthorhombic crystal from
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 | 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 | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 38 |
Details | binding site for residue NAP A 201 |
Chain | Residue |
A | TRP8 |
A | ARG46 |
A | ARG47 |
A | THR48 |
A | SER51 |
A | VAL67 |
A | THR68 |
A | ARG69 |
A | GLN70 |
A | GLY82 |
A | ILE100 |
A | ALA9 |
A | GLY102 |
A | ALA103 |
A | GLN104 |
A | ILE105 |
A | TYR106 |
A | LEU108 |
A | ALA132 |
A | WPD202 |
A | HOH328 |
A | HOH333 |
A | ILE16 |
A | HOH334 |
A | HOH342 |
A | HOH344 |
A | HOH346 |
A | HOH361 |
A | HOH369 |
A | HOH383 |
A | HOH424 |
A | HOH448 |
A | GLY17 |
A | ARG18 |
A | GLY20 |
A | GLY21 |
A | ILE22 |
A | GLY45 |
site_id | AC2 |
Number of Residues | 18 |
Details | binding site for residue WPD A 202 |
Chain | Residue |
A | ILE7 |
A | TRP8 |
A | ILE22 |
A | ASP29 |
A | LEU30 |
A | PHE33 |
A | LYS34 |
A | LEU52 |
A | PRO53 |
A | LEU59 |
A | ARG62 |
A | ILE100 |
A | TYR106 |
A | NAP201 |
A | HOH313 |
A | HOH416 |
B | ARG25 |
B | SER153 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CL A 203 |
Chain | Residue |
A | ARG25 |
A | LEU26 |
A | LEU30 |
B | ARG25 |
B | HOH527 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CL A 204 |
Chain | Residue |
A | ARG25 |
B | ARG25 |
B | LEU26 |
B | LEU30 |
B | HOH527 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue CL A 205 |
Chain | Residue |
A | ARG25 |
B | ILE22 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue CL B 201 |
Chain | Residue |
A | ILE22 |
A | ARG25 |
B | ARG25 |
B | HOH494 |
site_id | AC7 |
Number of Residues | 37 |
Details | binding site for residue NAP B 202 |
Chain | Residue |
B | HOH335 |
B | HOH336 |
B | HOH337 |
B | HOH350 |
B | HOH354 |
B | HOH370 |
B | HOH375 |
B | HOH385 |
B | HOH387 |
B | HOH425 |
A | ASP129 |
A | HOH357 |
B | TRP8 |
B | ALA9 |
B | ILE16 |
B | GLY17 |
B | ARG18 |
B | GLY20 |
B | GLY21 |
B | GLY45 |
B | ARG46 |
B | ARG47 |
B | THR48 |
B | SER51 |
B | VAL67 |
B | THR68 |
B | ARG69 |
B | GLN70 |
B | GLY82 |
B | ILE100 |
B | GLY102 |
B | ALA103 |
B | GLN104 |
B | ILE105 |
B | TYR106 |
B | ALA132 |
B | WPD203 |
site_id | AC8 |
Number of Residues | 19 |
Details | binding site for residue WPD B 203 |
Chain | Residue |
A | ARG25 |
A | SER153 |
B | ILE7 |
B | TRP8 |
B | ILE22 |
B | ASP29 |
B | LEU30 |
B | PHE33 |
B | LYS34 |
B | LEU52 |
B | PRO53 |
B | HIS56 |
B | LEU59 |
B | ARG62 |
B | ILE100 |
B | TYR106 |
B | NAP202 |
B | HOH321 |
B | HOH424 |
Functional Information from PROSITE/UniProt
site_id | PS00075 |
Number of Residues | 23 |
Details | DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGrdggIPWrlpe.DlahFkrlT |
Chain | Residue | Details |
A | VAL15-THR37 |