X-ray diffraction
1.6Å resolution

X-ray crystal Structure of E.coli Dihydrofolate Reductase complexed with folate and NADP+ at pH7.0


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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 18.02 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 34.293Å b: 45.625Å c: 98.974Å
α: 90° β: 90° γ: 90°
R R work R free
0.157 0.155 0.189
Expression system: Escherichia coli BL21(DE3)