PDBe 1j3j

X-ray diffraction
2.3Å resolution

Double mutant (C59R+S108N) Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) complexed with pyrimethamine, NADPH, and dUMP

Released:

Function and Biology Details

Reactions catalysed:
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bifunctional dihydrofolate reductase-thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 280 amino acids
Theoretical weight: 33.21 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P13922 (Residues: 1-280; Coverage: 46%)
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A
Bifunctional dihydrofolate reductase-thymidylate synthase Chains: C, D
Molecule details ›
Chains: C, D
Length: 328 amino acids
Theoretical weight: 38.71 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW P13922 (Residues: 281-608; Coverage: 54%)
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 56.343Å b: 154.999Å c: 164.001Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.231
Expression system: Escherichia coli BL21(DE3)