Entry | Database: PDB / ID: 7x73 |
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Title | Structure of G9a in complex with RK-701 |
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Components | Histone-lysine N-methyltransferase EHMT2 |
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Keywords | TRANSFERASE / histone lysine methyltransferase / inhibitor / protein-inhibitor complex |
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Function / homology | Function and homology information
regulation of protein modification process / histone H3K56 methyltransferase activity / phenotypic switching / neuron fate specification / [histone H3]-lysine9 N-methyltransferase / histone H3K9 methyltransferase activity / histone H3K9me2 methyltransferase activity / peptidyl-lysine dimethylation / histone H3K27 methyltransferase activity / synaptonemal complex assembly ...regulation of protein modification process / histone H3K56 methyltransferase activity / phenotypic switching / neuron fate specification / [histone H3]-lysine9 N-methyltransferase / histone H3K9 methyltransferase activity / histone H3K9me2 methyltransferase activity / peptidyl-lysine dimethylation / histone H3K27 methyltransferase activity / synaptonemal complex assembly / negative regulation of autophagosome assembly / DNA methylation-dependent heterochromatin formation / oocyte development / protein-lysine N-methyltransferase activity / C2H2 zinc finger domain binding / fertilization / cellular response to cocaine / negative regulation of gene expression via chromosomal CpG island methylation / organ growth / Transcriptional Regulation by E2F6 / regulation of DNA replication / RNA Polymerase I Transcription Initiation / behavioral response to cocaine / Transcriptional Regulation by VENTX / spermatid development / long-term memory / response to fungicide / cellular response to starvation / Transferases; Transferring one-carbon groups; Methyltransferases / transcription corepressor binding / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / promoter-specific chromatin binding / RNA polymerase II transcription regulatory region sequence-specific DNA binding / Regulation of TP53 Activity through Methylation / PKMTs methylate histone lysines / p53 binding / cellular response to xenobiotic stimulus / Senescence-Associated Secretory Phenotype (SASP) / response to ethanol / nuclear speck / chromatin / enzyme binding / negative regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleusSimilarity search - Function Histone-lysine N-methyltransferase EHMT2 / Histone-lysine N-methyltransferase EHMT1/EHMT2 / : / Histone-lysine N-methyltransferase EHMT1/EHMT2, Cys-rich region / Pre-SET domain / Pre-SET motif / Pre-SET domain profile. / N-terminal to some SET domains / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / SET domain superfamily ...Histone-lysine N-methyltransferase EHMT2 / Histone-lysine N-methyltransferase EHMT1/EHMT2 / : / Histone-lysine N-methyltransferase EHMT1/EHMT2, Cys-rich region / Pre-SET domain / Pre-SET motif / Pre-SET domain profile. / N-terminal to some SET domains / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / SET domain superfamily / SET domain / SET domain profile. / SET domain / Ankyrin repeat / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamilySimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.49 Å |
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Authors | Niwa, H. / Shirai, F. / Sato, S. / Nishigaya, Y. / Shirouzu, M. / Umehara, T. |
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Funding support | 1items Organization | Grant number | Country |
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Not funded | | |
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Citation | Journal: Nat Commun / Year: 2023 Title: A specific G9a inhibitor unveils BGLT3 lncRNA as a universal mediator of chemically induced fetal globin gene expression. Authors: Takase, S. / Hiroyama, T. / Shirai, F. / Maemoto, Y. / Nakata, A. / Arata, M. / Matsuoka, S. / Sonoda, T. / Niwa, H. / Sato, S. / Umehara, T. / Shirouzu, M. / Nishigaya, Y. / Sumiya, T. / ...Authors: Takase, S. / Hiroyama, T. / Shirai, F. / Maemoto, Y. / Nakata, A. / Arata, M. / Matsuoka, S. / Sonoda, T. / Niwa, H. / Sato, S. / Umehara, T. / Shirouzu, M. / Nishigaya, Y. / Sumiya, T. / Hashimoto, N. / Namie, R. / Usui, M. / Ohishi, T. / Ohba, S.I. / Kawada, M. / Hayashi, Y. / Harada, H. / Yamaguchi, T. / Shinkai, Y. / Nakamura, Y. / Yoshida, M. / Ito, A. |
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History | Deposition | Mar 9, 2022 | Deposition site: PDBJ / Processing site: PDBJ |
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Revision 1.0 | Dec 21, 2022 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jan 25, 2023 | Group: Database references / Category: citation / citation_author Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name |
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Revision 1.2 | Nov 29, 2023 | Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model |
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