X-ray diffraction
2.2Å resolution

Function and Biology Details

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
  • 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 R work R free
0.173 0.17 0.224
Expression system: Escherichia coli