› 1nja

X-ray diffraction
2.5Å resolution

THYMIDYLATE SYNTHASE, MUTATION, N229C WITH 2'-DEOXYCYTIDINE 5'-MONOPHOSPHATE (DCMP)

Released:
DOI: 10.2210/pdb1nja/pdb
PDB entry 1nja coloured by chain, front view.
PDB entry 1nja coloured by chain, side view.
PDB entry 1nja coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase.
Finer-Moore JS, Liu L, Schafmeister CE, Birdsall DL, Mau T, Santi DV, Stroud RM
Biochemistry 35 5125-36 (1996)
PMID: 8611496

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: 36.62 KDa
Source organism: Lacticaseibacillus casei
Expression system: Escherichia coli
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 DCM 1 x DCM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6122
Unit cell:
a: 78.7Å b: 78.7Å c: 230.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Thymidylate synthase inhibition: a structure-based rationale for drug design.
Costi MP. (1998)
7 other articles

1 mention without citation

Binding pocket optimization by computational protein design.
Malisi et al. (2012)