1dds

X-ray diffraction
2.2Å resolution

MOLECULE: DIHYDROFOLATE REDUCTASE (E.C.1.5.1.3) COMPLEXED WITH METHOTREXATE

Released:
Source organism: Escherichia coli
Primary publication:
The effect of denaturants on protein structure.
Protein Sci. 6 1727-33 (1997)
PMID: 9260285

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.02 KDa
Source organism: Escherichia coli
Expression system: [Clostridium] polysaccharolyticum
UniProt:
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P61
Unit cell:
a: 93.181Å b: 93.185Å c: 73.886Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.177 0.2
Expression system: [Clostridium] polysaccharolyticum