4o1x

X-ray diffraction
2.32Å resolution

Crystal structure of human thymidylate synthase double mutant C195S-Y202C

Released:
Source organism: Homo sapiens
Entry authors: Pozzi C, Mangani S

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Thymidylate synthase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 325 amino acids
Theoretical weight: 37.29 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: D
Molecule details ›
Chain: D
Length: 325 amino acids
Theoretical weight: 37.34 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

3 bound ligands:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 94.93Å b: 95.52Å c: 131.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.26
Expression system: Escherichia coli