› 1jtu

X-ray diffraction
2.2Å resolution

E. coli Thymidylate Synthase in a Complex with dUMP and LY338913, A Polyglutamylated Pyrrolo(2,3-d)pyrimidine-based Antifolate

Released:
DOI: 10.2210/pdb1jtu/pdb
PDB entry 1jtu coloured by chain, front view.
PDB entry 1jtu coloured by chain, side view.
PDB entry 1jtu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Multi-targeted antifolates aimed at avoiding drug resistance form covalent closed inhibitory complexes with human and Escherichia coli thymidylate synthases.
Sayre PH, Finer-Moore JS, Fritz TA, Biermann D, Gates SB, MacKellar WC, Patel VF, Stroud RM
J Mol Biol 313 813-29 (2001)
PMID: 11697906

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: 264 amino acids
Theoretical weight: 30.56 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 2 x UMP
Ligand LYB 2 x LYB
1 modified residue:
Ligand CXM 2 x CXM

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P63
Unit cell:
a: 127.6Å b: 127.6Å c: 68Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.198 0.241
Expression system: Escherichia coli

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Citations

2 review citations

Structure-based studies on species-specific inhibition of thymidylate synthase.
Costi et al. (2002)
1 more