4jef

X-ray diffraction
2.31Å resolution

Crystal structure of human thymidylate synthase Y202A in inactive conformation.

Released:

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 32.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04818 (Residues: 26-311; Coverage: 91%)
Gene names: OK/SW-cl.29, TS, TYMS
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P3121
Unit cell:
a: 95.955Å b: 95.955Å c: 82.649Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.185 0.222
Expression system: Escherichia coli