› 3v9p

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + dTMP = ADP + dTDP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173958 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 227 amino acids
Theoretical weight: 25.41 KDa
Source organism: Burkholderia thailandensis E264
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2SWM4 (Residues: 1-206; Coverage: 100%)
Gene names: BTH_I2154, tmk
Sequence domains: Thymidylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

4 bound ligands:
Ligand MRD 2 x MRD
Ligand GOL 2 x GOL
Ligand ACT 2 x ACT
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 68.13Å b: 77.97Å c: 84.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

2 mentions without citation

Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh et al. (2013)
1 more