› 1ddu

X-ray diffraction
2.1Å resolution

E. COLI THYMIDYLATE SYNTHASE IN COMPLEX WITH CB3717 AND 2',5'-DIDEOXYURIDINE (DDURD)

Released:
DOI: 10.2210/pdb1ddu/pdb
PDB entry 1ddu coloured by chain, front view.
PDB entry 1ddu coloured by chain, side view.
PDB entry 1ddu 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 Chains: A, B
Molecule details ›
Chains: A, B
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

3 bound ligands:
Ligand PO4 2 x PO4
Ligand DDU 2 x DDU
Ligand CB3 2 x CB3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P63
Unit cell:
a: 127.405Å b: 127.405Å c: 68.203Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 0.272
Expression system: Escherichia coli

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Citations

6 review citations

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