1o24

X-ray diffraction
2Å resolution

Crystal structure of Thymidylate Synthase Complementing Protein (TM0449) from Thermotoga maritima at 2.0 A resolution

Released:

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavin-dependent thymidylate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 232 amino acids
Theoretical weight: 27.5 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYT0 (Residues: 1-220; Coverage: 100%)
Gene names: TM_0449, thy1, thyX
Structure domains: Gyrase A; domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 54.48Å b: 116.639Å c: 142.252Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.252
Expression system: Escherichia coli