› 5ios

X-ray diffraction
1.9Å resolution

Flavin-dependent thymidylate synthase R90A variant in complex with FAD and deoxyuridine monophosphate

Released:
DOI: 10.2210/pdb5ios/pdb
PDB entry 5ios coloured by chain, front view.
PDB entry 5ios coloured by chain, side view.
PDB entry 5ios coloured by chain, top view.
Source organism: Thermotoga maritima MSB8
Primary publication:
Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase.
Stull FW, Bernard SM, Sapra A, Smith JL, Zuiderweg ER, Palfey BA
Biochemistry 55 3261-9 (2016)
PMID: 27214228

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: 27.42 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 4 x FAD
1 bound ligand:
Ligand UMP 4 x UMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 54.071Å b: 116.217Å c: 141.007Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.211
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Flavins as Covalent Catalysts: New Mechanisms Emerge.
Piano et al. (2017)
3 more