› 2orw

X-ray diffraction
1.5Å resolution

Thermotoga maritima thymidine kinase 1 like enzyme in complex with TP4A

Released:
DOI: 10.2210/pdb2orw/pdb
PDB 2orw coloured by chain and viewed from the front.
PDB 2orw coloured by chain and viewed from the side.
PDB 2orw coloured by chain and viewed from the top.
Source organism: Thermotoga maritima
Primary publication:
Binding of ATP to TK1-like enzymes is associated with a conformational change in the quaternary structure.
Segura-Peña D, Lutz S, Monnerjahn C, Konrad M, Lavie A
J. Mol. Biol. 369 129-41 (2007)
PMID: 17407781

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidine kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 20.68 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYN2 (Residues: 1-184; Coverage: 100%)
Gene names: TM_0401, tdk
Sequence domains: Thymidine kinase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 2 x MG
Ligand 4TA 2 x 4TA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 102.55Å b: 59.63Å c: 61.44Å
α: 90° β: 103.11° γ: 90°
R-values:
R R work R free
0.173 0.169 0.208
Expression system: Escherichia coli

Quick links

Citations

2 review citations

N3-substituted thymidine bioconjugates for cancer therapy and imaging.
Khalil et al. (2013)
1 more

5 mentions without citation

Prediction of structures of zinc-binding proteins through explicit modeling of metal coordination geometry.
Wang et al. (2010)
4 more