1bdu

X-ray diffraction
2.1Å resolution

E. COLI THYMIDYLATE SYNTHASE COMPLEXED WITH DURD

Released:
Source organism: Escherichia coli
Primary publication:
The additivity of substrate fragments in enzyme-ligand binding.
Structure 6 839-48 (1998)
PMID: 9687366

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
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 30.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: I213
Unit cell:
a: 133.05Å b: 133.05Å c: 133.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.237
Expression system: Escherichia coli