› 3tvl

X-ray diffraction
2.3Å resolution

Complex between the human thiamine triphosphatase and triphosphate

Released:
DOI: 10.2210/pdb3tvl/pdb
PDB entry 3tvl coloured by chain, front view.
PDB entry 3tvl coloured by chain, side view.
PDB entry 3tvl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase.
Delvaux D, Kerff F, Murty MR, Lakaye B, Czerniecki J, Kohn G, Wins P, Herman R, Gabelica V, Heuze F, Tordoir X, Marée R, Matagne A, Charlier P, De Pauw E, Bettendorff L
Biochim Biophys Acta 1830 4513-23 (2013)
PMID: 23707715

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-189727 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiamine-triphosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 230 amino acids
Theoretical weight: 25.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BU02 (Residues: 1-230; Coverage: 100%)
Gene name: THTPA
Sequence domains: CYTH domain
Structure domains: Hypothetical Protein Pfu-838710-001

Ligands and Environments

2 bound ligands:
Ligand 3PO 2 x 3PO
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 46.378Å b: 63.529Å c: 70.95Å
α: 90° β: 108.75° γ: 90°
R-values:
R R work R free
0.184 0.18 0.261
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

Update on Thiamine Triphosphorylated Derivatives and Metabolizing Enzymatic Complexes.
Bettendorff L. (2021)