1Q5U
HUMAN DUTP PYROPHOSPHATASE
Summary for 1Q5U
Entry DOI | 10.2210/pdb1q5u/pdb |
Related | 1Q5H |
Descriptor | dUTP pyrophosphatase (2 entities in total) |
Functional Keywords | dna repair, enzyme-dna interactions, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Isoform 1: Mitochondrion. Isoform 2: Nucleus: P33316 |
Total number of polymer chains | 3 |
Total formula weight | 48732.83 |
Authors | Mol, C.D.,Harris, J.M.,Mcintosh, E.M.,Tainer, J.A. (deposition date: 2003-08-11, release date: 2003-08-19, Last modification date: 2023-08-16) |
Primary citation | Mol, C.D.,Harris, J.M.,Mcintosh, E.M.,Tainer, J.A. Human dUTP Pyrophosphatase: Uracil Recognition by a Beta Hairpin and Active Sites Formed by Three Separate Subunits Structure, 4:1077-1092, 1996 Cited by PubMed Abstract: The essential enzyme dUTP pyrophosphatase (dUTPase) is exquisitely specific for dUTP and is critical for the fidelity of DNA replication and repair. dUTPase hydrolyzes dUTP to dUMP and pyrophosphate, simultaneously reducing dUTP levels and providing the dUMP for dTTP biosynthesis. A high cellular dTTP: dUTP ratio is essential to avoid uracil incorporation into DNA, which would lead to strand breaks and cell death. We report the first detailed atomic-resolution structure of a eukaryotic dUTPase, human dUTPase, and complexes with the uracil-containing deoxyribonucleotides, dUMP, dUDP and dUTP. PubMed: 8805593DOI: 10.1016/S0969-2126(96)00114-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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