X-ray diffraction
1.75Å resolution

pcDHFR K37S/F69N double mutant TMP NADPH ternary complex


Function and Biology Details

Reaction catalysed:
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Dihydrofolate reductase Chain: X
Molecule details ›
Chain: X
Length: 204 amino acids
Theoretical weight: 23.38 KDa
Source organism: Pneumocystis jirovecii
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P16184 (Residues: 3-206; Coverage: 99%)
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

Cofactor: Ligand NDP 1 x NDP
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 37.157Å b: 42.783Å c: 59.172Å
α: 90° β: 94.78° γ: 90°
R R work R free
0.261 0.259 0.316
Expression system: Escherichia coli BL21(DE3)