1f4d

X-ray diffraction
2.15Å resolution

CRYSTAL STRUCTURE OF E. COLI THYMIDYLATE SYNTHASE C146S, L143C COVALENTLY MODIFIED AT C143 WITH N-[TOSYL-D-PROLINYL]AMINO-ETHANETHIOL

Released:
Source organism: Escherichia coli
Primary publication:
Site-directed ligand discovery.
Proc. Natl. Acad. Sci. U.S.A. 97 9367-72 (2000)
PMID: 10944209

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (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
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P63
Unit cell:
a: 126.33Å b: 126.33Å c: 67.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.196 0.267
Expression system: Escherichia coli