2I5D
Crystal Structure of Human Inosine Triphosphate Pyrophosphatase
Summary for 2I5D
| Entry DOI | 10.2210/pdb2i5d/pdb |
| Related | 2CAR |
| Descriptor | inosine triphosphate pyrophosphohydrolase (2 entities in total) |
| Functional Keywords | monomeric protein, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : Q9BY32 |
| Total number of polymer chains | 1 |
| Total formula weight | 21750.90 |
| Authors | Porta, J.C.,Kozmin, S.G.,Pavlov, Y.I.,Borgstahl, G.E.O. (deposition date: 2006-08-24, release date: 2006-09-05, Last modification date: 2023-08-30) |
| Primary citation | Porta, J.,Kolar, C.,Kozmin, S.G.,Pavlov, Y.I.,Borgstahl, G.E.O. Structure of the orthorhombic form of human inosine triphosphate pyrophosphatase. Acta Crystallogr.,Sect.F, 62:1076-1081, 2006 Cited by PubMed Abstract: The structure of human inosine triphosphate pyrophosphohydrolase (ITPA) has been determined using diffraction data to 1.6 A resolution. ITPA contributes to the accurate replication of DNA by cleansing cellular dNTP pools of mutagenic nucleotide purine analogs such as dITP or dXTP. A similar high-resolution unpublished structure has been deposited in the Protein Data Bank from a monoclinic and pseudo-merohedrally twinned crystal. Here, cocrystallization of ITPA with a molar ratio of XTP appears to have improved the crystals by eliminating twinning and resulted in an orthorhombic space group. However, there was no evidence for bound XTP in the structure. Comparison with substrate-bound NTPase from a thermophilic organism predicts the movement of residues within helix alpha1, the loop before alpha6 and helix alpha7 to cap off the active site when substrate is bound. PubMed: 17077483DOI: 10.1107/S1744309106041790 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
Download full validation report
