› 2tdm

X-ray diffraction
2.55Å resolution

STRUCTURE OF THYMIDYLATE SYNTHASE

Released:
DOI: 10.2210/pdb2tdm/pdb
PDB entry 2tdm coloured by chain, front view.
PDB entry 2tdm coloured by chain, side view.
PDB entry 2tdm coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei.
Finer-Moore J, Fauman EB, Foster PG, Perry KM, Santi DV, Stroud RM
J Mol Biol 232 1101-16 (1993)
PMID: 8371269

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 36.63 KDa
Source organism: Lacticaseibacillus casei
Expression system: Escherichia coli
UniProt:
  • Canonical: P00469 (Residues: 1-316; Coverage: 100%)
Gene name: thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:
Ligand UMP 1 x UMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6122
Unit cell:
a: 78.6Å b: 78.6Å c: 240.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Thymidylate synthase: structure, inhibition, and strained conformations during catalysis.
Montfort et al. (1997)
3 more

2 mentions without citation

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 et al. (2019)
1 more