3tmk

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF YEAST THYMIDYLATE KINASE COMPLEXED WITH THE BISUBSTRATE INHIBITOR TP5A AT 2.0 A RESOLUTION: IMPLICATIONS FOR CATALYSIS AND AZT ACTIVATION

Released:

Function and Biology Details

Reaction catalysed:
ATP + dTMP = ADP + dTDP
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate kinase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 216 amino acids
Theoretical weight: 24.72 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00572 (Residues: 1-216; Coverage: 100%)
Gene names: CDC8, J1715, YJR057W
Sequence domains: Thymidylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P21
Unit cell:
a: 72.57Å b: 87.32Å c: 155.02Å
α: 90° β: 90.1° γ: 90°
R-values:
R R work R free
0.209 0.209 0.279