X-ray diffraction
2.61Å resolution

Crystal structure of DfrA5 dihydrofolate reductase in complex with TRIMETHOPRIM and NADPH


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Dihydrofolate reductase type 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 157 amino acids
Theoretical weight: 17.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P11731 (Residues: 1-157; Coverage: 100%)
Gene name: dhfrV
Sequence domains: Dihydrofolate reductase

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: NSLS BEAMLINE X25
Spacegroup: P43
Unit cell:
a: 99.53Å b: 99.53Å c: 42.82Å
α: 90° β: 90° γ: 90°
R R work R free
0.18 0.177 0.224
Expression system: Escherichia coli