› 1fwm

X-ray diffraction
2.2Å resolution

Crystal structure of the thymidylate synthase R166Q mutant

Released:
DOI: 10.2210/pdb1fwm/pdb
PDB entry 1fwm coloured by chain, front view.
PDB entry 1fwm coloured by chain, side view.
PDB entry 1fwm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of thymidylate synthase mutant R166Q: structural basis for the nearly complete loss of catalytic activity.
Sotelo-Mundo RR, Changchien L, Maley F, Montfort WR
J Biochem Mol Toxicol 20 88-92 (2006)
PMID: 16615077

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-141681 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 30.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A884 (Residues: 1-264; Coverage: 100%)
Gene names: JW2795, b2827, thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand CB3 2 x CB3
1 modified residue:
Ligand CXM 2 x CXM

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P63
Unit cell:
a: 127.06Å b: 127.06Å c: 67.67Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.225
Expression system: Escherichia coli

Quick links

Citations

2 review citations

5-Fluorouracil: mechanisms of resistance and reversal strategies.
Zhang et al. (2008)
1 more

1 mention without citation

Concerted versus stepwise mechanism in thymidylate synthase.
Islam et al. (2014)