› 2vet

X-ray diffraction
2.2Å 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-141681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 264 amino acids
Theoretical weight: 30.56 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A884 (Residues: 1-264; Coverage: 100%)
Gene names: JW2795, b2827, thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:
Ligand UMP 1 x UMP
1 modified residue:
Ligand CXM 1 x CXM

Experiments and Validation Details

Entry percentile scores
Spacegroup: I213
Unit cell:
a: 132.87Å b: 132.87Å c: 132.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.205
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Survey of the year 2008: applications of isothermal titration calorimetry.
Falconer et al. (2010)
1 more

1 mention without citation

Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant.
Arvizu-Flores et al. (2008)