› 2ccg

X-ray diffraction
2.3Å resolution

Crystal structure of His-tagged S. aureus thymidylate kinase complexed with thymidine monophosphate (TMP)

Released:
DOI: 10.2210/pdb2ccg/pdb
PDB entry 2ccg coloured by chain, front view.
PDB entry 2ccg coloured by chain, side view.
PDB entry 2ccg coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structures of S. aureus thymidylate kinase reveal an atypical active site configuration and an intermediate conformational state upon substrate binding.
Kotaka M, Dhaliwal B, Ren J, Nichols CE, Angell R, Lockyer M, Hawkins AR, Stammers DK
Protein Sci 15 774-84 (2006)
PMID: 16522804

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 225 amino acids
Theoretical weight: 25.63 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P65248 (Residues: 1-205; Coverage: 100%)
Gene names: SAV0482, tmk
Sequence domains: Thymidylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand TMP 2 x TMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 54.54Å b: 51.27Å c: 72.94Å
α: 90° β: 103.63° γ: 90°
R-values:
R R work R free
0.2 0.2 0.246
Expression system: Escherichia coli

Quick links

Citations

13 citation in other articles

Crystal structure of poxvirus thymidylate kinase: an unexpected dimerization has implications for antiviral therapy.
Caillat et al. (2008)
12 more

4 mentions without citation

Structural basis of generic versus specific E2-RING E3 interactions in protein ubiquitination.
Gundogdu et al. (2019)
3 more