6ezb

X-ray diffraction
2.25Å resolution

Crystal Structure of human tRNA-dihydrouridine(20) synthase catalytic domain Q305K mutant

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-192677 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA-dihydrouridine(20) synthase [NAD(P)+]-like Chain: A
Molecule details ›
Chain: A
Length: 327 amino acids
Theoretical weight: 36.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NX74 (Residues: 14-333; Coverage: 65%)
Gene names: DUS2, DUS2L
Sequence domains: Dihydrouridine synthase (Dus)

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: I222
Unit cell:
a: 72.08Å b: 84.11Å c: 144.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.223
Expression system: Escherichia coli