3qg2

X-ray diffraction
2.3Å resolution

Plasmodium falciparum DHFR-TS qradruple mutant (N51I+C59R+S108N+I164L, V1/S) pyrimethamine complex

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional dihydrofolate reductase-thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 608 amino acids
Theoretical weight: 71.91 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: D9N170 (Residues: 1-608; Coverage: 100%)
Gene names: DHFR-TS, V1/S
Sequence domains:
Structure domains:

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: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 56.486Å b: 155.272Å c: 164.995Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.233
Expression system: Escherichia coli