X-ray diffraction
1.15Å resolution

Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Dihydrofolate reductase type 2 Chain: A
Molecule details ›
Chain: A
Length: 62 amino acids
Theoretical weight: 6.74 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P00383 (Residues: 17-78; Coverage: 80%)
Sequence domains: R67 dihydrofolate reductase
Structure domains: SH3 type barrels.

Ligands and Environments

Cofactor: Ligand NAP 1 x NAP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: I4122
Unit cell:
a: 67.46Å b: 67.46Å c: 52.86Å
α: 90° β: 90° γ: 90°
R R work R free
0.195 0.19 0.215
Expression system: Escherichia coli