› 1thy

X-ray diffraction
2.9Å resolution

REFINED STRUCTURES OF SUBSTRATE-BOUND AND PHOSPHATE-BOUND THYMIDYLATE SYNTHASE FROM LACTOBACILLUS CASEI

Released:
DOI: 10.2210/pdb1thy/pdb
PDB entry 1thy coloured by chain, front view.
PDB entry 1thy coloured by chain, side view.
PDB entry 1thy coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei.
Finer-Moore J, Fauman EB, Foster PG, Perry KM, Santi DV, Stroud RM
J Mol Biol 232 1101-16 (1993)
PMID: 8371269

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-132544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 36.63 KDa
Source organism: Lacticaseibacillus casei
Expression system: Not provided
UniProt:
  • Canonical: P00469 (Residues: 1-316; Coverage: 100%)
Gene name: thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

1 bound ligand:
Ligand UMP 1 x UMP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6122
Unit cell:
a: 78.8Å b: 78.8Å c: 230.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Thymidylate synthase: structure, inhibition, and strained conformations during catalysis.
Montfort et al. (1997)
3 more

1 mention without citation

PMFF: Development of a Physics-Based Molecular Force Field for Protein Simulation and Ligand Docking.
Hwang et al. (2020)