4gyh

X-ray diffraction
3Å resolution

Structure of human thymidylate synthase at high salt conditions

Released:
Source organism: Homo sapiens
Primary publication:
Analysis of mRNA recognition by human thymidylate synthase.
Biosci Rep 34 e00168 (2014)
PMID: 25423174

Function and Biology Details

Reaction catalysed:
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:

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: 318 amino acids
Theoretical weight: 36.45 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 96.194Å b: 96.194Å c: 83.275Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.222 0.215 0.28
Expression system: Escherichia coli