登録情報 | データベース: PDB / ID: 3vnv |
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タイトル | Complex structure of viral RNA polymerase II |
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要素 | - Elongation factor Ts, Elongation factor Tu, LINKER, Q beta replicase
- RNA (5'-R(*CP*CP*CP*UP*AP*CP*C)-3')
- RNA (5'-R(*GP*GP*GP*UP*AP*GP*GP*G)-3')
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キーワード | TRANSLATION (翻訳 (生物学)) / TRANSFERASE/RNA / RNA POLYMERASE (RNAポリメラーゼ) / TRANSFERASE-RNA COMPLEX |
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機能・相同性 | 機能・相同性情報
guanosine tetraphosphate binding / translation elongation factor activity / RNA依存性RNAポリメラーゼ / viral RNA genome replication / RNA-dependent RNA polymerase activity / response to antibiotic / nucleotide binding / GTPase activity / GTP binding / RNA binding ...guanosine tetraphosphate binding / translation elongation factor activity / RNA依存性RNAポリメラーゼ / viral RNA genome replication / RNA-dependent RNA polymerase activity / response to antibiotic / nucleotide binding / GTPase activity / GTP binding / RNA binding / metal ion binding / 細胞膜 / 細胞質類似検索 - 分子機能 RNA-directed RNA polymerase beta-chain / RNA replicase, beta-chain / Translation elongation factor EFTs/EF1B / Translation elongation factor EFTs/EF1B, dimerisation / Translation elongation factor Ts, conserved site / Elongation factor Ts, dimerisation domain superfamily / Elongation factor TS / Elongation factor Ts signature 1. / Elongation factor Ts signature 2. / RNA-directed RNA polymerase, bacteriophage, catalytic domain ...RNA-directed RNA polymerase beta-chain / RNA replicase, beta-chain / Translation elongation factor EFTs/EF1B / Translation elongation factor EFTs/EF1B, dimerisation / Translation elongation factor Ts, conserved site / Elongation factor Ts, dimerisation domain superfamily / Elongation factor TS / Elongation factor Ts signature 1. / Elongation factor Ts signature 2. / RNA-directed RNA polymerase, bacteriophage, catalytic domain / RdRp of RNA-containing bacteriophages catalytic domain profile. / Translation elongation factor EFTu/EF1A, bacterial/organelle / Elongation factor Tu, domain 2 / Elongation factor Tu (EF-Tu), GTP-binding domain / Translation elongation factor EFTu/EF1A, C-terminal / Elongation factor Tu C-terminal domain / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / UBA-like superfamily / Translation factors / Tr-type G domain, conserved site / Translational (tr)-type guanine nucleotide-binding (G) domain signature. / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Elongation Factor Tu (Ef-tu); domain 3 / Small GTP-binding protein domain / Translation protein, beta-barrel domain superfamily / P-loop containing nucleotide triphosphate hydrolases / DNA/RNA polymerase superfamily / Βバレル / P-loop containing nucleoside triphosphate hydrolase / ロスマンフォールド / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta類似検索 - ドメイン・相同性 3'-DEOXY-CYTIDINE-5'-TRIPHOSPHATE / リボ核酸 / EF-Tu / Elongation factor Ts / RNA-directed RNA polymerase subunit beta類似検索 - 構成要素 |
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生物種 | Escherichia coli O157:H7 (大腸菌) Escherichia phage Qbeta (ファージ) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.604 Å |
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データ登録者 | Takeshita, D. / Tomita, K. |
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引用 | ジャーナル: Structure / 年: 2012 タイトル: Mechanism for template-independent terminal adenylation activity of Q beta replicase 著者: Takeshita, D. / Yamashita, S. / Tomita, K. |
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履歴 | 登録 | 2012年1月18日 | 登録サイト: PDBJ / 処理サイト: PDBJ |
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改定 1.0 | 2012年8月8日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2013年10月9日 | Group: Database references |
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改定 1.2 | 2017年6月28日 | Group: Source and taxonomy / カテゴリ: entity_src_gen |
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改定 1.3 | 2023年11月8日 | Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Refinement description カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / 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.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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