› 2ja1

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + thymidine = ADP + thymidine 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170945 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidine kinase Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 21.87 KDa
Source organism: Bacillus cereus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0H0H6 (Residues: 1-195; Coverage: 100%)
Gene names: AT268_20020, B4081_4809, BKK64_12090, BLX06_03770, C1N66_11430, C6A78_14085, CN357_30570, CN980_06535, COC69_01765, COI98_09330, COK98_18730, CON36_03255, D0437_26050, DR116_0009955, F8172_17950, FC695_06390, NCTC7464_02567, TQ94_05640, tdk, tdk2
Sequence domains: Thymidine kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand TTP 1 x TTP
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I4122
Unit cell:
a: 95.39Å b: 95.39Å c: 204.862Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.239
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Carboranyl thymidine analogues for neutron capture therapy.
Tjarks et al. (2007)
1 more

3 mentions without citation

Tracking in atomic detail the functional specializations in viral RecA helicases that occur during evolution.
El Omari et al. (2013)
2 more