X-ray diffraction
2.71Å resolution

Thymidylate synthase from Staphylococcus aureus.

Entry authors: Osipiuk J, Holowicki J, Jedrzejczak R, Rubin E, Guinn K, Ioerger T, Baker D, Sacchettini J, Joachimiak A, Midwest Center for Structural Genomics (MCSG), Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 321 amino acids
Theoretical weight: 37.14 KDa
Source organism: Staphylococcus aureus subsp. aureus Mu50
Expression system: Escherichia coli
  • Canonical: P67046 (Residues: 1-318; Coverage: 100%)
Gene names: SAV1427, thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P43
Unit cell:
a: 111.309Å b: 111.309Å c: 59.081Å
α: 90° β: 90° γ: 90°
R R work R free
0.195 0.192 0.252
Expression system: Escherichia coli