› 2tsr

X-ray diffraction
2.6Å resolution

THYMIDYLATE SYNTHASE FROM RAT IN TERNARY COMPLEX WITH DUMP AND TOMUDEX

Released:
DOI: 10.2210/pdb2tsr/pdb
PDB entry 2tsr coloured by chain, front view.
PDB entry 2tsr coloured by chain, side view.
PDB entry 2tsr coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug.
Sotelo-Mundo RR, Ciesla J, Dzik JM, Rode W, Maley F, Maley GF, Hardy LW, Montfort WR
Biochemistry 38 1087-94 (1999)
PMID: 9894005

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-545643 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 307 amino acids
Theoretical weight: 35.06 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P45352 (Residues: 1-307; Coverage: 100%)
Gene name: Tyms
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

2 bound ligands:
Ligand UMP 4 x UMP
Ligand D16 4 x D16
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 99.7Å b: 101.6Å c: 140.8Å
α: 90° β: 101.4° γ: 90°
R-values:
R R work R free
0.162 0.162 0.222
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Targeting Methyltransferases in Human Pathogenic Bacteria: Insights into Thymidylate Synthase (TS) and Flavin-Dependent TS (FDTS).
Pozzi et al. (2019)
19 other articles

2 mentions without citation

Crystal structure of mouse thymidylate synthase in tertiary complex with dUMP and raltitrexed reveals N-terminus architecture and two different active site conformations.
Dowierciał et al. (2014)
1 more