› 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:
DOI: 10.2210/pdb3tmk/pdb
PDB entry 3tmk coloured by chain, front view.
PDB entry 3tmk coloured by chain, side view.
PDB entry 3tmk coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of yeast thymidylate kinase complexed with the bisubstrate inhibitor P1-(5'-adenosyl) P5-(5'-thymidyl) pentaphosphate (TP5A) at 2.0 A resolution: implications for catalysis and AZT activation.
Lavie A, Konrad M, Brundiers R, Goody RS, Schlichting I, Reinstein J
Biochemistry 37 3677-86 (1998)
PMID: 9521686

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132724 (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:
Ligand T5A 8 x T5A
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

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Citations

1 review citation

The enantioselectivity of enzymes involved in current antiviral therapy using nucleoside analogues: a new strategy?
Maury G. (2000)
38 other articles

3 mentions without citation

From the similarity analysis of protein cavities to the functional classification of protein families using cavbase.
Kuhn et al. (2006)
2 more