3n5e

X-ray diffraction
2.26Å resolution

Crystal Structure of human thymidylate synthase bound to a peptide inhibitor

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.31 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
Thymidylate synthase Chain: B
Molecule details ›
Chain: B
Length: 325 amino acids
Theoretical weight: 37.26 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
Synthetic peptide LR Chain: D
Molecule details ›
Chain: D
Length: 8 amino acids
Theoretical weight: 1.01 KDa

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P31
Unit cell:
a: 96.109Å b: 96.109Å c: 82.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.188 0.221
Expression system: Escherichia coli