4gta

X-ray diffraction
1.5Å resolution

T. Maritima FDTS with FAD, dUMP, and Folinic Acid

Released:
Source organism: Thermotoga maritima MSB8
Primary publication:
Folate binding site of flavin-dependent thymidylate synthase.
Proc Natl Acad Sci U S A 109 15722-7 (2012)
PMID: 23019356

Function and Biology Details

Reaction catalysed:
5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-194544 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin-dependent thymidylate synthase Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 27.5 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYT0 (Residues: 1-220; Coverage: 100%)
Gene names: TM_0449, thy1, thyX
Sequence domains: Thymidylate synthase complementing protein
Structure domains: Gyrase A; domain 2

Ligands and Environments


Cofactor: Ligand FFO 1 x FFO

Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: I4122
Unit cell:
a: 110.3Å b: 110.3Å c: 121.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.179
Expression system: Escherichia coli