X-ray diffraction
1.56Å resolution

Structure of closed state of Dihydrofolate reductase from Mycobacterium tuberculosis in complex with NADPH and pyrimethamine


Function and Biology Details

Reaction catalysed:
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 17.66 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
  • Canonical: P9WNX1 (Residues: 3-161; Coverage: 99%)
Gene names: MTV002.28c, Rv2763c, dfrA, folA
Sequence domains: Dihydrofolate reductase

Ligands and Environments

Cofactor: Ligand NDP 2 x NDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 60.505Å b: 71.372Å c: 72.373Å
α: 90° β: 90° γ: 90°
R R work R free
0.179 0.177 0.21
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'