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1Q5H

Human dUTP Pyrophosphatase complex with dUDP

Summary for 1Q5H
Entry DOI10.2210/pdb1q5h/pdb
DescriptordUTP pyrophosphatase, MAGNESIUM ION, DEOXYURIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
Functional Keywordsdna repair, enzyme-dna interactions, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationIsoform 1: Mitochondrion. Isoform 2: Nucleus: P33316
Total number of polymer chains3
Total formula weight49921.62
Authors
Mol, C.D.,Harris, J.M.,McIntosh, E.M.,Tainer, J.A. (deposition date: 2003-08-07, release date: 2003-08-19, Last modification date: 2023-08-16)
Primary citationMol, 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: 8805593
DOI: 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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