› 4eck

X-ray diffraction
3.52Å resolution

Function and Biology Details

Reactions catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170468 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional dihydrofolate reductase-thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 610 amino acids
Theoretical weight: 68.84 KDa
Source organism: Toxoplasma gondii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07422 (Residues: 1-610; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
3 bound ligands:
Ligand UMP 2 x UMP
Ligand CB3 2 x CB3
Ligand FOL 2 x FOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2
Unit cell:
a: 185.944Å b: 143.015Å c: 59.84Å
α: 90° β: 90.02° γ: 90°
R-values:
R R work R free
0.335 0.332 0.395
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Substrate channelling as an approach to cascade reactions.
Wheeldon et al. (2016)
2 more

2 mentions without citation

Dihydrofolate reductase, thymidylate synthase, and serine hydroxy methyltransferase: successful targets against some infectious diseases.
Shamshad et al. (2022)
1 more