› 1trg

X-ray diffraction
1.9Å resolution

E. COLI THYMIDYLATE SYNTHASE IN SYMMETRIC COMPLEX WITH CB3717 AND 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP)

Released:
DOI: 10.2210/pdb1trg/pdb
PDB entry 1trg coloured by chain, front view.
PDB entry 1trg coloured by chain, side view.
PDB entry 1trg coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The additivity of substrate fragments in enzyme-ligand binding.
Stout TJ, Sage CR, Stroud RM
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:
Sequence domains:
Structure domain:

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: 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:
Ligand UMP 1 x UMP
Ligand CB3 1 x CB3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3121
Unit cell:
a: 71.96Å b: 71.96Å c: 115.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.23
Expression system: Escherichia coli

Quick links

Citations

6 review citations

High-throughput crystallography for lead discovery in drug design.
Blundell et al. (2002)
5 more

3 mentions without citation

Explaining an unusually fast parasitic enzyme: folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase.
Martucci et al. (2008)
2 more