› 1ufq

X-ray diffraction
2.5Å resolution

Crystal structure of ligand-free human uridine-cytidine kinase 2

Released:
DOI: 10.2210/pdb1ufq/pdb
PDB entry 1ufq coloured by chain, front view.
PDB entry 1ufq coloured by chain, side view.
PDB entry 1ufq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase.
Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F
Structure 12 751-64 (2004)
PMID: 15130468

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-189869 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridine-cytidine kinase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 252 amino acids
Theoretical weight: 28.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9BZX2 (Residues: 1-250; Coverage: 96%)
Gene names: UCK2, UMPK
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 BL44XU
Spacegroup: P21212
Unit cell:
a: 84.057Å b: 94.262Å c: 156.989Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.236 0.287
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Regulation of mammalian nucleotide metabolism and biosynthesis.
Lane et al. (2015)
3 more

1 mention without citation

Prediction of the tetramer protein complex interaction based on CNN and SVM.
Lyu et al. (2023)