登録情報 | データベース: PDB / ID: 3pt9 |
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タイトル | Crystal structure of mouse DNMT1(731-1602) in the free state |
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要素 | DNA (cytosine-5)-methyltransferase 1 |
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キーワード | TRANSFERASE / Maintenance DNA methylation |
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機能・相同性 | 機能・相同性情報
SUMOylation of DNA methylation proteins / chromosomal DNA methylation maintenance following DNA replication / negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching / epigenetic programming of gene expression / PRC2 methylates histones and DNA / DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates / cellular response to bisphenol A / DNA-methyltransferase activity / negative regulation of vascular associated smooth muscle cell apoptotic process / DNA (cytosine-5-)-methyltransferase ...SUMOylation of DNA methylation proteins / chromosomal DNA methylation maintenance following DNA replication / negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching / epigenetic programming of gene expression / PRC2 methylates histones and DNA / DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates / cellular response to bisphenol A / DNA-methyltransferase activity / negative regulation of vascular associated smooth muscle cell apoptotic process / DNA (cytosine-5-)-methyltransferase / DNA (cytosine-5-)-methyltransferase activity / S-adenosylmethionine metabolic process / female germ cell nucleus / methyl-CpG binding / DNA methylation-dependent heterochromatin formation / lncRNA binding / germ cell nucleus / negative regulation of gene expression via chromosomal CpG island methylation / heterochromatin / pericentric heterochromatin / cellular response to transforming growth factor beta stimulus / positive regulation of vascular associated smooth muscle cell proliferation / replication fork / methyltransferase activity / promoter-specific chromatin binding / nuclear estrogen receptor binding / cellular response to amino acid stimulus / histone deacetylase binding / regulation of cell population proliferation / regulation of gene expression / methylation / response to xenobiotic stimulus / protein domain specific binding / negative regulation of gene expression / negative regulation of DNA-templated transcription / DNA-templated transcription / chromatin binding / positive regulation of gene expression / negative regulation of transcription by RNA polymerase II / enzyme binding / protein-containing complex / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus / cytoplasm類似検索 - 分子機能 Bromo adjacent homology (BAH) domain / DNA (cytosine-5)-methyltransferase 1-like / DNA (cytosine-5)-methyltransferase 1, replication foci domain / Cytosine specific DNA methyltransferase replication foci domain / DMAP1-binding Domain / DMAP1-binding Domain / DNA Methylase, subunit A, domain 2 / DMAP1-binding domain / DMAP1-binding domain profile. / DNA Methylase; Chain A, domain 2 ...Bromo adjacent homology (BAH) domain / DNA (cytosine-5)-methyltransferase 1-like / DNA (cytosine-5)-methyltransferase 1, replication foci domain / Cytosine specific DNA methyltransferase replication foci domain / DMAP1-binding Domain / DMAP1-binding Domain / DNA Methylase, subunit A, domain 2 / DMAP1-binding domain / DMAP1-binding domain profile. / DNA Methylase; Chain A, domain 2 / : / DNA methylase, C-5 cytosine-specific, conserved site / C-5 cytosine-specific DNA methylases C-terminal signature. / CXXC zinc finger domain / DNA methylase, C-5 cytosine-specific, active site / C-5 cytosine-specific DNA methylases active site. / Zinc finger, CXXC-type / Zinc finger CXXC-type profile. / C-5 cytosine-specific DNA methylase (Dnmt) domain profile. / C-5 cytosine methyltransferase / C-5 cytosine-specific DNA methylase / Bromo adjacent homology domain / BAH domain / Bromo adjacent homology (BAH) domain superfamily / Bromo adjacent homology (BAH) domain / BAH domain profile. / Vaccinia Virus protein VP39 / SH3 type barrels. / Roll / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Alpha-Beta Complex / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta類似検索 - ドメイン・相同性 S-ADENOSYL-L-HOMOCYSTEINE / DNA (cytosine-5)-methyltransferase 1類似検索 - 構成要素 |
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生物種 | ![](img/tx_mammal.gif) Mus musculus (ハツカネズミ) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.5 Å |
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データ登録者 | Song, J. / Patel, D.J. |
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引用 | ジャーナル: Science / 年: 2011 タイトル: Structure of DNMT1-DNA complex reveals a role for autoinhibition in maintenance DNA methylation. 著者: Song, J. / Rechkoblit, O. / Bestor, T.H. / Patel, D.J. |
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履歴 | 登録 | 2010年12月2日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2010年12月29日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2011年7月13日 | Group: Version format compliance |
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改定 1.2 | 2024年2月21日 | Group: Data collection / Database references / Derived calculations カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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