› 1f4f

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF E. COLI THYMIDYLATE SYNTHASE COMPLEXED WITH SP-722

Released:
DOI: 10.2210/pdb1f4f/pdb
PDB entry 1f4f coloured by chain, front view.
PDB entry 1f4f coloured by chain, side view.
PDB entry 1f4f coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Site-directed ligand discovery.
Erlanson DA, Braisted AC, Raphael DR, Randal M, Stroud RM, Gordon EM, Wells JA
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:
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: 30.56 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 5 x SO4
Ligand TP3 2 x TP3
1 modified residue:
Ligand CXM 2 x CXM

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P63
Unit cell:
a: 126.14Å b: 126.14Å c: 66.812Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.194 0.251
Expression system: Escherichia coli

Quick links

Citations

69 review citations

Small-molecule inhibitors of protein-protein interactions: progressing towards the dream.
Arkin et al. (2004)
68 more

3 mentions without citation

Site-directed ligand discovery.
Erlanson et al. (2000)
2 more