› 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:
DOI: 10.2210/pdb5uiv/pdb
PDB entry 5uiv coloured by chain, front view.
PDB entry 5uiv coloured by chain, side view.
PDB entry 5uiv coloured by chain, top view.
Source organism: Candida albicans SC5314
Primary publication:
The Structure of Thymidylate Kinase from Candida albicans Reveals a Unique Structural Element.
Sinha K, Rule GS
Biochemistry 56 4360-4370 (2017)
PMID: 28742342

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-176853 (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, orf19.8730
Sequence domains: Thymidylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand TMP 1 x TMP
Ligand ADP 1 x ADP
Ligand MG 2 x MG
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

Quick links

Citations

1 review citation

Protein-Protein Interactions in Candida albicans.
Schoeters et al. (2019)
3 other articles

3 mentions without citation

Docking Prediction, Antifungal Activity, Anti-Biofilm Effects on Candida spp., and Toxicity against Human Cells of Cinnamaldehyde.
da Nóbrega Alves et al. (2020)
2 more