› 3asy

X-ray diffraction
2.4Å resolution

ligand-free structure of uridine kinase from thermus thermophilus HB8

Released:
DOI: 10.2210/pdb3asy/pdb
PDB entry 3asy coloured by chain, front view.
PDB entry 3asy coloured by chain, side view.
PDB entry 3asy coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
A single amino acid limits the substrate specificity of Thermus thermophilus uridine-cytidine kinase to cytidine.
Tomoike F, Nakagawa N, Kuramitsu S, Masui R
Biochemistry 50 4597-607 (2011)
PMID: 21539325

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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-values:
R R work R free
0.233 0.233 0.3
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach.
Mestrom et al. (2019)
1 more

1 mention without citation

α-Galactosidase and Sucrose-Kinase Relationships in a Bi-functional AgaSK Enzyme Produced by the Human Gut Symbiont Ruminococcus gnavus E1.
Lafond et al. (2020)