› 4e28

X-ray diffraction
2.3Å resolution

Structure of human thymidylate synthase in inactive conformation with a novel non-peptidic inhibitor

Released:
DOI: 10.2210/pdb4e28/pdb
PDB entry 4e28 coloured by chain, front view.
PDB entry 4e28 coloured by chain, side view.
PDB entry 4e28 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inhibitor of ovarian cancer cells growth by virtual screening: a new thiazole derivative targeting human thymidylate synthase.
Carosati E, Tochowicz A, Marverti G, Guaitoli G, Benedetti P, Ferrari S, Stroud RM, Finer-Moore J, Luciani R, Farina D, Cruciani G, Costi MP
J Med Chem 55 10272-6 (2012)
PMID: 23075414

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-138196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04818 (Residues: 1-313; Coverage: 100%)
Gene names: OK/SW-cl.29, TS, TYMS
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand 0MZ 1 x 0MZ
Ligand 9MZ 1 x 9MZ
1 modified residue:
Ligand CME 2 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P3121
Unit cell:
a: 95.747Å b: 95.747Å c: 82.407Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.188 0.229
Expression system: Escherichia coli

Quick links

Citations

15 citation in other articles

Isozyme-specific ligands for O-acetylserine sulfhydrylase, a novel antibiotic target.
Spyrakis et al. (2013)
14 more