› 3ob7

X-ray diffraction
2.75Å resolution

Human Thymidylate Synthase R163K with Cys 195 covalently modified by Glutathione

Released:
DOI: 10.2210/pdb3ob7/pdb
PDB entry 3ob7 coloured by chain, front view.
PDB entry 3ob7 coloured by chain, side view.
PDB entry 3ob7 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


Cofactor: Ligand GSH 2 x GSH
1 bound ligand:
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 201.798Å b: 123.106Å c: 99.928Å
α: 90° β: 115.75° γ: 90°
R-values:
R R work R free
0.234 0.234 0.293
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

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