Entry | Database: PDB / ID: 5ans |
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Title | Potent and selective inhibitors of MTH1 probe its role in cancer cell survival |
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Components | 7,8-DIHYDRO-8-OXOGUANINE TRIPHOSPHATASE |
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Keywords | HYDROLASE / MTH1 / ONCOLOGY / NUCLEOTIDE HYDROLYSIS / INHIBITION |
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Function / homology | Function and homology information
2-hydroxy-ATP hydrolase activity / 2-hydroxy-dATP hydrolase activity / N6-methyl-(d)ATP hydrolase activity / O6-methyl-dGTP hydrolase activity / 2-hydroxy-dATP diphosphatase / dATP diphosphatase activity / ATP diphosphatase activity / 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity ...2-hydroxy-ATP hydrolase activity / 2-hydroxy-dATP hydrolase activity / N6-methyl-(d)ATP hydrolase activity / O6-methyl-dGTP hydrolase activity / 2-hydroxy-dATP diphosphatase / dATP diphosphatase activity / ATP diphosphatase activity / 8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity / hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides / 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity / DNA protection / Phosphate bond hydrolysis by NUDT proteins / purine nucleoside catabolic process / snoRNA binding / Hydrolases; Acting on acid anhydrides; In phosphorus-containing anhydrides / response to cadmium ion / acrosomal vesicle / male gonad development / nuclear membrane / response to oxidative stress / mitochondrial matrix / DNA repair / mitochondrion / extracellular space / nucleus / metal ion binding / cytosol / cytoplasmSimilarity search - Function Oxidized purine nucleoside triphosphate / NUDIX hydrolase / NUDIX hydrolase, conserved site / Nudix box signature. / Nucleoside Triphosphate Pyrophosphohydrolase / Nucleoside Triphosphate Pyrophosphohydrolase / NUDIX domain / Nudix hydrolase domain profile. / NUDIX hydrolase domain / NUDIX hydrolase-like domain superfamily ...Oxidized purine nucleoside triphosphate / NUDIX hydrolase / NUDIX hydrolase, conserved site / Nudix box signature. / Nucleoside Triphosphate Pyrophosphohydrolase / Nucleoside Triphosphate Pyrophosphohydrolase / NUDIX domain / Nudix hydrolase domain profile. / NUDIX hydrolase domain / NUDIX hydrolase-like domain superfamily / Alpha-Beta Complex / Alpha BetaSimilarity search - Domain/homology |
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Biological species | HOMO SAPIENS (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å |
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Authors | Kettle, J.G. / Alwan, H. / Bista, M. / Breed, J. / Kack, H. / Eckersley, K. / Foote, K.M. / Fillery, S. / Goodwin, L. / Jones, D. ...Kettle, J.G. / Alwan, H. / Bista, M. / Breed, J. / Kack, H. / Eckersley, K. / Foote, K.M. / Fillery, S. / Goodwin, L. / Jones, D. / Lau, A. / Nissink, J.W.M. / Read, J. / Scott, J. / Taylor, B. / Walker, G. / Wissler, L. |
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Citation | Journal: J.Med.Chem. / Year: 2016 Title: Potent and Selective Inhibitors of Mth1 Probe its Role in Cancer Cell Survival. Authors: Kettle, J.G. / Alwan, H. / Bista, M. / Breed, J. / Davies, N.L. / Eckersley, K. / Fillery, S. / Foote, K.M. / Goodwin, L. / Jones, D.R. / Kack, H. / Lau, A. / Nissink, J.W. / Read, J. / ...Authors: Kettle, J.G. / Alwan, H. / Bista, M. / Breed, J. / Davies, N.L. / Eckersley, K. / Fillery, S. / Foote, K.M. / Goodwin, L. / Jones, D.R. / Kack, H. / Lau, A. / Nissink, J.W. / Read, J. / Scott, J.S. / Taylor, B. / Walker, G. / Wissler, L. / Wylot, M. |
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History | Deposition | Sep 8, 2015 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Mar 2, 2016 | Provider: repository / Type: Initial release |
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Revision 1.1 | Apr 6, 2016 | Group: Database references |
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Revision 1.2 | May 8, 2024 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_site Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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