› 5fuw

X-ray diffraction
2.2Å resolution

catalytic domain of Thymidine kinase from Trypanosoma brucei with dTMP or dThd

Released:
DOI: 10.2210/pdb5fuw/pdb
PDB entry 5fuw coloured by chain, front view.
PDB entry 5fuw coloured by chain, side view.
PDB entry 5fuw coloured by chain, top view.
Source organism: Trypanosoma brucei
Primary publication:
Cell cycle regulation and novel structural features of thymidine kinase, an essential enzyme in Trypanosoma brucei.
Valente M, Timm J, Castillo-Acosta VM, Ruiz-Pérez LM, Balzarini T, Nettleship JE, Bird LE, Rada H, Wilson KS, González-Pacanowska D
Mol Microbiol 102 365-385 (2016)
PMID: 27426054

Function and Biology Details

Reaction catalysed: 
ATP + thymidine = ADP + thymidine 5'-phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174409 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
thymidine kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 182 amino acids
Theoretical weight: 20.5 KDa
Source organism: Trypanosoma brucei
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q38CF2 (Residues: 203-384; Coverage: 40%)
Gene name: Tb10.70.7270
Sequence domains: Thymidine kinase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand QBT 1 x QBT
Ligand PO4 3 x PO4
Ligand ZN 2 x ZN
Ligand THM 1 x THM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P4322
Unit cell:
a: 114.999Å b: 114.999Å c: 104.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.201
Expression system: Spodoptera frugiperda

Quick links

Citations

6 citation in other articles

Proteomic Analysis of the Cell Cycle of Procylic Form Trypanosoma brucei.
Crozier et al. (2018)
5 more