登録情報 データベース : PDB / ID : 2bzs 構造の表示 ダウンロードとリンクタイトル Binding of anti-cancer prodrug CB1954 to the activating enzyme NQO2 revealed by the crystal structure of their complex. 要素NRH DEHYDROGENASE [QUINONE] 2 詳細 キーワード OXIDOREDUCTASE / NQO2 / CB1954 / FAD / FLAVOPROTEIN / METAL-BINDING / POLYMORPHISM / ZINC機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
ribosyldihydronicotinamide dehydrogenase (quinone) / dihydronicotinamide riboside quinone reductase activity / quinone catabolic process / resveratrol binding / oxidoreductase activity, acting on other nitrogenous compounds as donors / melatonin binding / NAD(P)H dehydrogenase (quinone) activity / Phase I - Functionalization of compounds / chloride ion binding / FAD binding ... ribosyldihydronicotinamide dehydrogenase (quinone) / dihydronicotinamide riboside quinone reductase activity / quinone catabolic process / resveratrol binding / oxidoreductase activity, acting on other nitrogenous compounds as donors / melatonin binding / NAD(P)H dehydrogenase (quinone) activity / Phase I - Functionalization of compounds / chloride ion binding / FAD binding / oxidoreductase activity / electron transfer activity / protein homodimerization activity / zinc ion binding / extracellular exosome / nucleoplasm / cytosol 類似検索 - 分子機能 : / Flavodoxin-like fold / Flavodoxin-like fold / Flavodoxin domain / Flavoprotein-like superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta 類似検索 - ドメイン・相同性 5-(AZIRIDIN-1-YL)-2,4-DINITROBENZAMIDE / FLAVIN-ADENINE DINUCLEOTIDE / Ribosyldihydronicotinamide dehydrogenase [quinone] 類似検索 - 構成要素生物種 HOMO SAPIENS (ヒト)手法 X線回折 / 分子置換 / 解像度 : 2 Å 詳細データ登録者 Abu Khader, M.M. / Heap, J.T. / De Matteis, C. / Kellam, B. / Doughty, S.W. / Minton, N. / Paoli, M. 引用ジャーナル : J.Med.Chem. / 年 : 2005タイトル : Binding of the Anticancer Prodrug Cb1954 to the Activating Enzyme Nqo2 Revealed by the Crystal Structure of Their Complex.著者 : Abu Khader, M.M. / Heap, J.T. / De Matteis, C. / Kellam, B. / Doughty, S.W. / Minton, N. / Paoli, M. 履歴 登録 2005年8月22日 登録サイト : PDBE / 処理サイト : PDBE改定 1.0 2005年9月23日 Provider : repository / タイプ : Initial release改定 1.1 2011年5月8日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Version format compliance改定 1.3 2018年12月12日 Group : Advisory / Data collection / Structure summary / カテゴリ : chem_comp / pdbx_unobs_or_zero_occ_residues / Item : _chem_comp.pdbx_synonyms改定 1.4 2023年12月13日 Group : Advisory / Data collection ... Advisory / Data collection / Database references / Derived calculations / Other / Refinement description / Structure summary カテゴリ : chem_comp / chem_comp_atom ... chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_residues / struct_conn / 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 / _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.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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
すべて表示 表示を減らす Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.