› 5x4y

X-ray diffraction
2.2Å resolution

Mutant human thymidylate synthase M190K crystallized in a sulfate-containing condition

Released:
DOI: 10.2210/pdb5x4y/pdb
PDB entry 5x4y coloured by chain, front view.
PDB entry 5x4y coloured by chain, side view.
PDB entry 5x4y coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states.
Chen D, Jansson A, Sim D, Larsson A, Nordlund P
J Biol Chem 292 13449-13458 (2017)
PMID: 28634233

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: 314 amino acids
Theoretical weight: 35.85 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

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P3121
Unit cell:
a: 95.951Å b: 95.951Å c: 80.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.235
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential.
Zhao et al. (2021)
3 more

1 mention without citation

Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states.
Chen et al. (2017)