› 4jef

X-ray diffraction
2.31Å resolution

Crystal structure of human thymidylate synthase Y202A in inactive conformation.

Released:
DOI: 10.2210/pdb4jef/pdb
PDB entry 4jef coloured by chain, front view.
PDB entry 4jef coloured by chain, side view.
PDB entry 4jef coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Hotspots in an obligate homodimeric anticancer target. Structural and functional effects of interfacial mutations in human thymidylate synthase.
Salo-Ahen OM, Tochowicz A, Pozzi C, Cardinale D, Ferrari S, Boum Y, Mangani S, Stroud RM, Saxena P, Myllykallio H, Costi MP, Ponterini G, Wade RC
J Med Chem 58 3572-81 (2015)
PMID: 25798950

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: 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
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
1 modified residue:
Ligand CME 2 x CME

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

Quick links

Citations

2 review citations

Deoxyribonucleotide metabolism, mutagenesis and cancer.
Mathews CK. (2015)
1 more

1 mention without citation

Hotspots in an obligate homodimeric anticancer target. Structural and functional effects of interfacial mutations in human thymidylate synthase.
Salo-Ahen et al. (2015)