3TVL
Complex between the human thiamine triphosphatase and triphosphate
Summary for 3TVL
| Entry DOI | 10.2210/pdb3tvl/pdb |
| Related | 2jmu 3bhd |
| Descriptor | Thiamine-triphosphatase, TRIPHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | hydrolase, magnesium binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm: Q9BU02 |
| Total number of polymer chains | 2 |
| Total formula weight | 51891.85 |
| Authors | Delvaux, D.,Herman, R.,Sauvage, E.,Wins, P.,Bettendorff, L.,Charlier, P.,Kerff, F. (deposition date: 2011-09-20, release date: 2012-10-10, Last modification date: 2023-09-13) |
| Primary citation | Delvaux, D.,Kerff, F.,Murty, M.R.,Lakaye, B.,Czerniecki, J.,Kohn, G.,Wins, P.,Herman, R.,Gabelica, V.,Heuze, F.,Tordoir, X.,Maree, R.,Matagne, A.,Charlier, P.,De Pauw, E.,Bettendorff, L. Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase. Biochim.Biophys.Acta, 1830:4513-4523, 2013 Cited by PubMed Abstract: Thiamine triphosphate (ThTP) is present in most organisms and might be involved in intracellular signaling. In mammalian cells, the cytosolic ThTP level is controlled by a specific thiamine triphosphatase (ThTPase), belonging to the CYTH superfamily of proteins. CYTH proteins are present in all superkingdoms of life and act on various triphosphorylated substrates. PubMed: 23707715DOI: 10.1016/j.bbagen.2013.05.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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