› 4eiz

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydrofolate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.02 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABQ4 (Residues: 1-159; Coverage: 100%)
Gene names: JW0047, b0048, folA, tmrA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A
Nb113 Camel antibody fragment Chains: C, D
Molecule details ›
Chains: C, D
Length: 134 amino acids
Theoretical weight: 14.82 KDa
Source organism: Lama glama
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 101.361Å b: 77.517Å c: 93.473Å
α: 90° β: 91.28° γ: 90°
R-values:
R R work R free
0.173 0.17 0.224
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Chemical space of Escherichia coli dihydrofolate reductase inhibitors: New approaches for discovering novel drugs for old bugs.
Srinivasan et al. (2019)
2 more

2 mentions without citation

Detection and manipulation of live antigen-expressing cells using conditionally stable nanobodies.
Tang et al. (2016)
1 more