登録情報 データベース : PDB / ID : 1uuo 構造の表示 ダウンロードとリンクタイトル Rat dihydroorotate dehydrogenase (DHOD)in complex with brequinar 要素DIHYDROOROTATE DEHYDROGENASE 詳細 キーワード OXIDOREDUCTASE / DIHYDROOROTATE DEHYDROGENASE / BREQUINAR / ATOVAQUONE / NUCLEOTIDE METABOLISM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
Pyrimidine biosynthesis / response to L-arginine / pyrimidine ribonucleotide biosynthetic process / dihydroorotate dehydrogenase (quinone) activity / dihydroorotate dehydrogenase (quinone) / dihydroorotate dehydrogenase activity / dihydroorotase activity / UDP biosynthetic process / response to caffeine / regulation of mitochondrial fission ... Pyrimidine biosynthesis / response to L-arginine / pyrimidine ribonucleotide biosynthetic process / dihydroorotate dehydrogenase (quinone) activity / dihydroorotate dehydrogenase (quinone) / dihydroorotate dehydrogenase activity / dihydroorotase activity / UDP biosynthetic process / response to caffeine / regulation of mitochondrial fission / response to starvation / ubiquinone binding / 'de novo' UMP biosynthetic process / quinone binding / 'de novo' pyrimidine nucleobase biosynthetic process / lactation / female pregnancy / response to organic cyclic compound / FMN binding / mitochondrial inner membrane / response to xenobiotic stimulus / positive regulation of apoptotic process / neuronal cell body 類似検索 - 分子機能 Dihydroorotate dehydrogenase, class 2 / Dihydroorotate dehydrogenase signature 1. / Dihydroorotate dehydrogenase signature 2. / Dihydroorotate dehydrogenase, conserved site / : / Dihydroorotate dehydrogenase domain / Dihydroorotate dehydrogenase / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel ... Dihydroorotate dehydrogenase, class 2 / Dihydroorotate dehydrogenase signature 1. / Dihydroorotate dehydrogenase signature 2. / Dihydroorotate dehydrogenase, conserved site / : / Dihydroorotate dehydrogenase domain / Dihydroorotate dehydrogenase / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha Beta 類似検索 - ドメイン・相同性 Chem-BRF / FLAVIN MONONUCLEOTIDE / NICKEL (II) ION / OROTIC ACID / Dihydroorotate dehydrogenase (quinone), mitochondrial 類似検索 - 構成要素生物種 RATTUS RATTUS (エジプトネズミ)手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 2.44 Å 詳細データ登録者 Hansen, M. / Le Nours, J. / Johansson, E. / Antal, T. / Ullrich, A. / Loffler, M. / Larsen, S. 引用ジャーナル : Protein Sci. / 年 : 2004タイトル : Inhibitor Binding in a Class 2 Dihydroorotate Dehydrogenase Causes Variations in the Membrane-Associated N-Terminal Domain著者 : Hansen, M. / Le Nours, J. / Johansson, E. / Antal, T. / Ullrich, A. / Loffler, M. / Larsen, S. 履歴 登録 2004年1月8日 登録サイト : PDBE / 処理サイト : PDBE改定 1.0 2004年4月1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1月17日 Group : Data collection / カテゴリ : diffrn_source / Item : _diffrn_source.pdbx_synchrotron_site改定 1.4 2019年1月30日 Group : Data collection / Experimental preparation / カテゴリ : exptl_crystal_grow / Item : _exptl_crystal_grow.method改定 1.5 2024年5月8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 / struct_conn Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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
すべて表示 表示を減らす Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.