X-ray diffraction
1.9Å resolution

Crystal structure of Human tRNA dihydrouridine synthase 2

Source organism: Homo sapiens
Primary publication:
From bacterial to human dihydrouridine synthase: automated structure determination.
Acta Crystallogr. D Biol. Crystallogr. 71 1564-71 (2015)
PMID: 26143927

Function and Biology Details

Reaction catalysed:
5,6-dihydrouracil(20) in tRNA + NAD(P)(+) = uracil(20) in tRNA + NAD(P)H
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like Chain: A
Molecule details ›
Chain: A
Length: 346 amino acids
Theoretical weight: 38.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q9NX74 (Residues: 1-340; Coverage: 69%)
Gene names: DUS2, DUS2L
Sequence domains: Dihydrouridine synthase (Dus)

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21
Unit cell:
a: 46.252Å b: 49.562Å c: 69.612Å
α: 90° β: 95.71° γ: 90°
R R work R free
0.17 0.168 0.206
Expression system: Escherichia coli BL21(DE3)