X-ray diffraction
2.4Å resolution

ligand-free structure of uridine kinase from thermus thermophilus HB8


Function and Biology Details

Reaction catalysed:
ATP + cytidine = ADP + CMP
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Uridine kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 211 amino acids
Theoretical weight: 23.71 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
  • Canonical: Q5SKR5 (Residues: 1-211; Coverage: 100%)
Gene names: TTHA0578, udk
Sequence domains: Phosphoribulokinase / Uridine kinase family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P43212
Unit cell:
a: 70.364Å b: 70.364Å c: 179.243Å
α: 90° β: 90° γ: 90°
R R work R free
0.233 0.233 0.3
Expression system: Escherichia coli