› 3h9k

X-ray diffraction
2.65Å resolution

Structures of Thymidylate Synthase R163K with Substrates and Inhibitors Show Subunit Asymmetry

Released:
DOI: 10.2210/pdb3h9k/pdb
PDB entry 3h9k coloured by chain, front view.
PDB entry 3h9k coloured by chain, side view.
PDB entry 3h9k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human thymidylate synthase R163K with dUMP, FdUMP and glutathione show asymmetric ligand binding.
Gibson LM, Celeste LR, Lovelace LL, Lebioda L
Acta Crystallogr D Biol Crystallogr 67 60-6 (2011)
PMID: 21206062

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 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 313 amino acids
Theoretical weight: 35.73 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 UFP 3 x UFP
Ligand EDO 2 x EDO
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 200.284Å b: 122.19Å c: 99.828Å
α: 90° β: 115.18° γ: 90°
R-values:
R R work R free
0.214 0.214 0.26
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Analogues of Pyrimidine Nucleosides as Mycobacteria Growth Inhibitors.
Alexandrova et al. (2022)
5 other articles

4 mentions without citation

Structures of human thymidylate synthase R163K with dUMP, FdUMP and glutathione show asymmetric ligand binding.
Gibson et al. (2011)
3 more