3ld9

X-ray diffraction
2.15Å resolution

Crystal structure of thymidylate kinase from Ehrlichia chaffeensis at 2.15A resolution

Released:
Primary publication:
Structure of thymidylate kinase from Ehrlichia chaffeensis.
OpenAccess logo Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 1090-4 (2011)
PMID: 21904055

Function and Biology Details

Reaction catalysed:
ATP + dTMP = ADP + dTDP
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate kinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 223 amino acids
Theoretical weight: 25.51 KDa
Source organism: Ehrlichia chaffeensis str. Arkansas
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2GHN3 (Residues: 1-202; Coverage: 100%)
Gene names: ECH_0229, tmk
Sequence domains: Thymidylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 39.17Å b: 144.82Å c: 146.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.232
Expression system: Escherichia coli BL21(DE3)