› 6qya

X-ray diffraction
1.76Å resolution

Crystal structure of Enteroccocus faecalis thymidylate synthase (EfTS) in complex with dUMP

Released:
DOI: 10.2210/pdb6qya/pdb
PDB entry 6qya coloured by chain, front view.
PDB entry 6qya coloured by chain, side view.
PDB entry 6qya coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
Structural Comparison of Enterococcus faecalis and Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational Variabilities.
Pozzi C, Ferrari S, Luciani R, Tassone G, Costi MP, Mangani S
OpenAccess logo Molecules 24 (2019)
PMID: 30935102

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182801 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thymidylate synthase Chains: A, C
Molecule details ›
Chains: A, C
Length: 315 amino acids
Theoretical weight: 36.4 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q834R3 (Residues: 1-315; Coverage: 100%)
Gene names: EF_1576, thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain
Thymidylate synthase Chains: B, D
Molecule details ›
Chains: B, D
Length: 315 amino acids
Theoretical weight: 36.46 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q834R3 (Residues: 1-315; Coverage: 100%)
Gene names: EF_1576, thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments


Cofactor: Ligand FFO 2 x FFO
4 bound ligands:
Ligand UMP 2 x UMP
Ligand EDO 11 x EDO
Ligand SO4 3 x SO4
Ligand CL 1 x CL
2 modified residues:
Ligand CSX 2 x CSX
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 73.16Å b: 95.101Å c: 97.409Å
α: 90° β: 93.63° γ: 90°
R-values:
R R work R free
0.186 0.184 0.22
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Investigation of the Anticancer Effect of α-Aminophosphonates and Arylidine Derivatives of 3-Acetyl-1-aminoquinolin-2(1H)-one on the DMBA Model of Breast Cancer in Albino Rats with In Silico Prediction of Their Thymidylate Synthase Inhibitory Effect.
Nassan et al. (2022)
4 more

3 mentions without citation

Targeting Methyltransferases in Human Pathogenic Bacteria: Insights into Thymidylate Synthase (TS) and Flavin-Dependent TS (FDTS).
Pozzi et al. (2019)
2 more