› 2qq0

X-ray diffraction
1.5Å resolution

Thymidine Kinase from Thermotoga Maritima in complex with thymidine + AppNHp

Released:
DOI: 10.2210/pdb2qq0/pdb
PDB entry 2qq0 coloured by chain, front view.
PDB entry 2qq0 coloured by chain, side view.
PDB entry 2qq0 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes.
Segura-Peña D, Lichter J, Trani M, Konrad M, Lavie A, Lutz S
Structure 15 1555-66 (2007)
PMID: 18073106

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-194522 (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 BL21
UniProt:
  • Canonical: Q9WYN2 (Residues: 1-184; Coverage: 100%)
Gene names: TM_0401, tdk
Sequence domains: Thymidine kinase
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 2 x MG
Ligand THM 1 x THM
Ligand ANP 1 x ANP
Ligand TMP 1 x TMP
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 102.16Å b: 59.31Å c: 61.3Å
α: 90° β: 103.02° γ: 90°
R-values:
R R work R free
0.175 0.171 0.217
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

A survey of the year 2007 literature on applications of isothermal titration calorimetry.
Bjelić et al. (2008)
1 more

3 mentions without citation

Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes.
Segura-Peña et al. (2007)
2 more