› 5a64

X-ray diffraction
2.1Å resolution

Crystal structure of mouse thiamine triphosphatase in complex with thiamine triphosphate.

Released:
DOI: 10.2210/pdb5a64/pdb
PDB entry 5a64 coloured by chain, front view.
PDB entry 5a64 coloured by chain, side view.
PDB entry 5a64 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.
Martinez J, Truffault V, Hothorn M
J Biol Chem 290 23348-60 (2015)
PMID: 26221030

Function and Biology Details

Reaction catalysed: 
Thiamine triphosphate + H(2)O = thiamine diphosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185041 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiamine-triphosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 24.43 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8JZL3 (Residues: 1-224; Coverage: 100%)
Gene name: Thtpa
Sequence domains: CYTH domain
Structure domains: Hypothetical Protein Pfu-838710-001

Ligands and Environments

3 bound ligands:
Ligand V4E 2 x V4E
Ligand EDO 4 x EDO
Ligand PGE 2 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 103.181Å b: 93.578Å c: 70.775Å
α: 90° β: 93.04° γ: 90°
R-values:
R R work R free
0.212 0.211 0.232
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

mRNA capping: biological functions and applications.
Ramanathan et al. (2016)
1 more

1 mention without citation

Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.
Martinez et al. (2015)