› 2bl9

X-ray diffraction
1.9Å resolution

X-ray crystal structure of Plasmodium vivax dihydrofolate reductase in complex with pyrimethamine and its derivative

Released:
DOI: 10.2210/pdb2bl9/pdb
PDB entry 2bl9 coloured by chain, front view.
PDB entry 2bl9 coloured by chain, side view.
PDB entry 2bl9 coloured by chain, top view.
Source organism: Plasmodium vivax
Primary publication:
Crystal structure of dihydrofolate reductase from Plasmodium vivax: pyrimethamine displacement linked with mutation-induced resistance.
Kongsaeree P, Khongsuk P, Leartsakulpanich U, Chitnumsub P, Tarnchompoo B, Walkinshaw MD, Yuthavong Y
Proc Natl Acad Sci U S A 102 13046-51 (2005)
PMID: 16135570

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126417 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional dihydrofolate reductase-thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 27.11 KDa
Source organism: Plasmodium vivax
Expression system: Escherichia coli
UniProt:
  • Canonical: O02604 (Residues: 1-238; Coverage: 38%)
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
1 bound ligand:
Ligand CP6 1 x CP6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 134.28Å b: 55.74Å c: 45.72Å
α: 90° β: 107.09° γ: 90°
R-values:
R R work R free
0.208 0.208 0.26
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Targeting purine and pyrimidine metabolism in human apicomplexan parasites.
Hyde JE. (2007)
8 more

17 mentions without citation

How mutational epistasis impairs predictability in protein evolution and design.
Miton et al. (2016)
16 more