› 4o1u

X-ray diffraction
2.26Å resolution

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 325 amino acids
Theoretical weight: 37.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04818 (Residues: 1-313; Coverage: 100%)
Gene names: OK/SW-cl.29, TS, TYMS
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

3 bound ligands:
Ligand SO4 6 x SO4
Ligand EDO 4 x EDO
Ligand CL 3 x CL
2 modified residues:
Ligand SCH 6 x SCH
Ligand CME 4 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P31
Unit cell:
a: 96.23Å b: 96.23Å c: 83.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.172 0.21
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Destabilizers of the thymidylate synthase homodimer accelerate its proteasomal degradation and inhibit cancer growth.
Costantino et al. (2022)