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- SASDC57: Deoxyuridine 5'-triphosphate nucleotidohydrolase (hDUT) -

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Basic information

Entry
Database: SASBDB / ID: SASDC57
SampleDeoxyuridine 5'-triphosphate nucleotidohydrolase
  • Deoxyuridine 5'-triphosphate nucleotidohydrolase (protein), hDUT, Homo sapiens
Function / homology
Function and homology information


pyrimidine deoxyribonucleotide binding / dUTP catabolic process / dUMP biosynthetic process / dUTP diphosphatase / dUTP diphosphatase activity / Interconversion of nucleotide di- and triphosphates / peroxisome proliferator activated receptor binding / nucleobase-containing compound metabolic process / signaling receptor inhibitor activity / dTMP biosynthetic process ...pyrimidine deoxyribonucleotide binding / dUTP catabolic process / dUMP biosynthetic process / dUTP diphosphatase / dUTP diphosphatase activity / Interconversion of nucleotide di- and triphosphates / peroxisome proliferator activated receptor binding / nucleobase-containing compound metabolic process / signaling receptor inhibitor activity / dTMP biosynthetic process / regulation of protein-containing complex assembly / liver development / DNA replication / magnesium ion binding / mitochondrion / RNA binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus
Similarity search - Function
Deoxyuridine triphosphate nucleotidohydrolase / dUTPase-like / dUTPase / dUTPase, trimeric / dUTPase-like superfamily
Similarity search - Domain/homology
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationDate: 2018 Mar 12
Title: Structural model of human dUTPase in complex with a novel proteinaceous inhibitor
Authors: Nyíri K / Mertens H / Tihanyi B / Nagy G / Kőhegyi B / Matejka J / Harris M / Szabó J / Papp-Kádár V / Németh-Pongrácz V / Ozohanics O / Vékey K / Svergun D / Borysik A
Contact author
  • Haydyn Mertens (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #1489
Type: dummy / Software: (2.9.0) / Radius of dummy atoms: 2.10 A / Symmetry: P1 / Chi-square value: 1.000
Search similar-shape structures of this assembly by Omokage search (details)
Model #1490
Type: atomic / Software: (2.9.0) / Radius of dummy atoms: 1.90 A / Symmetry: P3 / Comment: Addition of terminal residues to PDB ID: 3EHW / Chi-square value: 1.059
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Deoxyuridine 5'-triphosphate nucleotidohydrolase / Dry vol: 21815 / Specimen concentration: 0.20-2.00 / Concentration method: A280
BufferName: 50 mM HEPES 300 mM NaCl 5 mM MgCl2 / pH: 7.5 / Comment: Buffer B
Entity #775Name: hDUT / Type: protein
Description: Deoxyuridine 5'-triphosphate nucleotidohydrolase
Formula weight: 18.029 / Num. of mol.: 3 / Source: Homo sapiens / References: UniProt: P33316
Sequence:
GSHMPCSEET PAISPSKRAR PAEVGGMQLR FARLSEHATA PTRGSARAAG YDLYSAYDYT IPPMEKAVVK TDIQIALPSG CYGRVAPRSG LAAKHFIDVG AGVIDEDYRG NVGVVLFNFG KEKFEVKKGD RIAQLICERI FYPEIEEVQA LDDTERGSGG FGSTGKN

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Experimental information

BeamInstrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: hDUT / Measurement date: Jul 9, 2016 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.1322 5.0307
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1200 /
MinMax
Q0.132242 3.43554
P(R) point1 1200
R0 10
Result
Type of curve: merged / Standard: water
ExperimentalExperimental errorStandardStandard errorPorodPorod errorEstimatedEstimated errorEstimated method
MW57.9 kDa6 35 kDa5 73 kDa7 ---
Volume----117 nm310 133 20 DAM volume

P(R)P(R) errorGuinierGuinier error
Forward scattering, I00.025 0.001 0.025 0.001
Radius of gyration, Rg2.94 nm0.1 3 nm0.1

MinMaxError
D-10 0.5
Guinier point1 93 -

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