PDBe 1j3k

X-ray diffraction
2.1Å resolution

Quadruple mutant (N51I+C59R+S108N+I164L) Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS) complexed with WR99210, NADPH, and dUMP

Released:

Function and Biology Details

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: 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: 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: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 59.679Å b: 158.093Å c: 165.738Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.182 0.222
Expression system: Escherichia coli BL21(DE3)