登録情報 | データベース: PDB / ID: 4s0r |
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タイトル | Structure of GS-TnrA complex |
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要素 | - Glutamine synthetase
- TnrA peptide
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キーワード | Ligase / chaperone / glutamine synthesis / transcription regulation |
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機能・相同性 | 機能・相同性情報
nitrogen catabolite activation of transcription / cellular response to nitrogen levels / glutamine binding / nitrogen catabolite repression of transcription / negative regulation of core promoter binding / glutamine synthetase / polyamine catabolic process / glutamine biosynthetic process / glutamine synthetase activity / glutamate binding ...nitrogen catabolite activation of transcription / cellular response to nitrogen levels / glutamine binding / nitrogen catabolite repression of transcription / negative regulation of core promoter binding / glutamine synthetase / polyamine catabolic process / glutamine biosynthetic process / glutamine synthetase activity / glutamate binding / core promoter sequence-specific DNA binding / DNA-binding transcription factor binding / negative regulation of DNA-templated transcription / magnesium ion binding / ATP binding / plasma membrane / cytoplasm類似検索 - 分子機能 Glutamine synthetase class-I, adenylation site / Glutamine synthetase class-I adenylation site. / Glutamine synthetase, N-terminal domain / Glutamine synthetase type I / Glutamine synthetase/guanido kinase, catalytic domain / Glutamine synthetase (GS) beta-grasp domain profile. / Glutamine synthetase (GS) catalytic domain profile. / Glutamine synthetase, N-terminal conserved site / Glutamine synthetase signature 1. / Glutamine synthetase, beta-Grasp domain ...Glutamine synthetase class-I, adenylation site / Glutamine synthetase class-I adenylation site. / Glutamine synthetase, N-terminal domain / Glutamine synthetase type I / Glutamine synthetase/guanido kinase, catalytic domain / Glutamine synthetase (GS) beta-grasp domain profile. / Glutamine synthetase (GS) catalytic domain profile. / Glutamine synthetase, N-terminal conserved site / Glutamine synthetase signature 1. / Glutamine synthetase, beta-Grasp domain / MerR HTH family regulatory protein / Creatine Kinase; Chain A, domain 2 / MerR-type HTH domain profile. / helix_turn_helix, mercury resistance / Glutamine synthetase, glycine-rich site / Glutamine synthetase putative ATP-binding region signature. / MerR-type HTH domain / Glutamine synthetase, N-terminal domain / Glutamine synthetase, N-terminal domain superfamily / Glutamine synthetase, catalytic domain / Glutamine synthetase, catalytic domain / Glutamine synthetase, catalytic domain / Glutamine synthetase/guanido kinase, catalytic domain / Putative DNA-binding domain superfamily / Ubiquitin-like (UB roll) / Roll / 2-Layer Sandwich / Alpha Beta類似検索 - ドメイン・相同性 GLUTAMINE / Glutamine synthetase / HTH-type transcriptional regulator TnrA類似検索 - 構成要素 |
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生物種 | ![](img/tx_bacteria.gif) Bacillus subtilis (枯草菌) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 3.5 Å |
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データ登録者 | Schumacher, M.A. / Chinnam, N.G. / Cuthbert, B. / Tonthat, N.K. |
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引用 | ジャーナル: Genes Dev. / 年: 2015 タイトル: Structures of regulatory machinery reveal novel molecular mechanisms controlling B. subtilis nitrogen homeostasis. 著者: Schumacher, M.A. / Chinnam, N.B. / Cuthbert, B. / Tonthat, N.K. / Whitfill, T. |
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履歴 | 登録 | 2015年1月4日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2015年3月4日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2017年11月22日 | Group: Refinement description / カテゴリ: software / Item: _software.name |
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改定 1.2 | 2024年2月28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_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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_asym_id / _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_asym_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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