5F9K
Dictyostelium discoideum dUTPase at 2.2 Angstrom
Summary for 5F9K
Entry DOI | 10.2210/pdb5f9k/pdb |
Descriptor | Deoxyuridine 5'-triphosphate nucleotidohydrolase, 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | hydrolase |
Biological source | Dictyostelium discoideum (Slime mold) |
Total number of polymer chains | 3 |
Total formula weight | 48243.76 |
Authors | Inoguchi, N.,Chia, C.P.,Heck, K.,Moriyama, H. (deposition date: 2015-12-09, release date: 2016-12-14, Last modification date: 2023-09-27) |
Primary citation | Chia, C.P.,Inoguchi, N.,Varon, K.C.,Bartholomai, B.M.,Moriyama, H. Mitochondrial localization of Dictyostelium discoideum dUTPase mediated by its N-terminus. Bmc Res Notes, 13:16-16, 2020 Cited by PubMed Abstract: The nuclear and mitochondrial genomes of Dictyostelium discoideum, a unicellular eukaryote, have relatively high A+T-contents of 77.5% and 72.65%, respectively. To begin to investigate how the pyrimidine biosynthetic pathway fulfills the demand for dTTP, we determined the catalytic properties and structure of the key enzyme deoxyuridine triphosphate nucleotidohydrolase (dUTPase) that hydrolyzes dUTP to dUMP, the precursor of dTTP. PubMed: 31910901DOI: 10.1186/s13104-019-4879-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.179 Å) |
Structure validation
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