› 4kas

X-ray diffraction
1.85Å resolution

Crystal structure of FDTS from T. maritima mutant (H53D) with FAD and dUMP

Released:
DOI: 10.2210/pdb4kas/pdb
PDB entry 4kas coloured by chain, front view.
PDB entry 4kas coloured by chain, side view.
PDB entry 4kas coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
Flavin-Dependent Thymidylate Synthase as a Drug Target for Deadly Microbes: Mutational Study and a Strategy for Inhibitor Design.
Mathews II
J Bioterror Biodef Suppl 12 004 (2013)
PMID: 24563811

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194544 (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: 27.48 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 FAD 2 x FAD
5 bound ligands:
Ligand DU 3 x DU
Ligand SO4 2 x SO4
Ligand CL 1 x CL
Ligand PO4 1 x PO4
Ligand 2PE 1 x 2PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 54.37Å b: 116.67Å c: 141.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.211
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Flavin-dependent thymidylate synthase: N5 of flavin as a Methylene carrier.
Karunaratne et al. (2017)
2 other articles

1 mention without citation

Flavin-Dependent Thymidylate Synthase as a Drug Target for Deadly Microbes: Mutational Study and a Strategy for Inhibitor Design.
Mathews II. (2013)