Summary for 4OOQ
| Entry DOI | 10.2210/pdb4ooq/pdb |
| Related | 4OOP |
| Descriptor | Deoxyuridine 5'-triphosphate nucleotidohydrolase, SULFATE ION, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | dutpase, hydrolysis, dutp, hydrolase |
| Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
| Total number of polymer chains | 3 |
| Total formula weight | 52953.01 |
| Authors | Inoguchi, N.,Bajaj, M.,Moriyama, H. (deposition date: 2014-02-03, release date: 2015-07-22, Last modification date: 2023-09-20) |
| Primary citation | Inoguchi, N.,Chaiseeda, K.,Yamanishi, M.,Kim, M.K.,Jang, Y.,Bajaj, M.,Chia, C.P.,Becker, D.F.,Moriyama, H. Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation. BMC Res Notes, 8:784-784, 2015 Cited by PubMed Abstract: Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) hydrolyzes dUTP to dUMP and pyrophosphate to maintain the cellular thymine-uracil ratio. dUTPase is also a target for cancer chemotherapy. However, the mechanism defining its substrate affinity remains unclear. Sequence comparisons of various dUTPases revealed that Arabidopsis thaliana dUTPase has a unique tryptophan at position 93, which potentially contributes to its degree of substrate affinity. To better understand the roles of tryptophan 93, A. thaliana dUTPase was studied. PubMed: 26666293DOI: 10.1186/s13104-015-1760-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.004 Å) |
Structure validation
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