› 2tdd

X-ray diffraction
2.7Å resolution

STRUCTURES OF THYMIDYLATE SYNTHASE WITH A C-TERMINAL DELETION: ROLE OF THE C-TERMINUS IN ALIGNMENT OF D/UMP AND CH2H4FOLATE

Released:
DOI: 10.2210/pdb2tdd/pdb
PDB entry 2tdd coloured by chain, front view.
PDB entry 2tdd coloured by chain, side view.
PDB entry 2tdd coloured by chain, top view.
Source organism: Lacticaseibacillus casei
Primary publication:
Structures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment of 2'-deoxyuridine 5'-monophosphate and 5,10-methylenetetrahydrofolate.
Perry KM, Carreras CW, Chang LC, Santi DV, Stroud RM
Biochemistry 32 7116-25 (1993)
PMID: 8343503

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: 315 amino acids
Theoretical weight: 36.53 KDa
Source organism: Lacticaseibacillus casei
Expression system: Not provided
UniProt:
  • Canonical: P00469 (Residues: 1-315; Coverage: 100%)
Gene name: thyA
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments


Cofactor: Ligand THF 1 x THF
1 bound ligand:
Ligand UFP 1 x UFP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6122
Unit cell:
a: 78.4Å b: 78.4Å c: 242.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

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Citations

2 review citations

Methylenetetrahydrofolate reductase: a common human polymorphism and its biochemical implications.
Matthews RG. (2002)
1 more