5uiv

X-ray diffraction
2.45Å resolution

Structure of Thymidylate Kinase from Candida albicans Reveals Origin of Broad Substrate Specificity and a Novel Structural Element.

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:
dTMP kinase Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 25.89 KDa
Source organism: Candida albicans SC5314
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59TV7 (Residues: 2-224; Coverage: 100%)
Gene names: CAALFM_C111790WA, orf19.1137
Sequence domains: Thymidylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: P3221
Unit cell:
a: 69.965Å b: 69.965Å c: 116.161Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.218
Expression system: Escherichia coli