› 2onb

X-ray diffraction
2.7Å resolution

Human Thymidylate Synthase at low salt conditions with PDPA bound

Released:
DOI: 10.2210/pdb2onb/pdb
PDB entry 2onb coloured by chain, front view.
PDB entry 2onb coloured by chain, side view.
PDB entry 2onb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cooperative inhibition of human thymidylate synthase by mixtures of active site binding and allosteric inhibitors.
Lovelace LL, Gibson LM, Lebioda L
Biochemistry 46 2823-30 (2007)
PMID: 17297914

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: 313 amino acids
Theoretical weight: 36.07 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 1 x SO4
Ligand EDO 1 x EDO
Ligand 7PA 1 x 7PA
1 modified residue:
Ligand CME 4 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P3121
Unit cell:
a: 95.69Å b: 95.69Å c: 82.503Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.259
Expression system: Escherichia coli

Quick links

Citations

19 citation in other articles

Protein-protein interface-binding peptides inhibit the cancer therapy target human thymidylate synthase.
Cardinale et al. (2011)
18 more

2 mentions without citation

Analysis of mRNA recognition by human thymidylate synthase.
Brunn et al. (2014)
1 more