登録情報 | データベース: PDB / ID: 6eyf |
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タイトル | Butyrylcolinesterase expressed in CHO cells co-crystallised with a rivastigmine analogue |
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要素 | Cholinesterase |
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キーワード | HYDROLASE / Butyrylcholinesterase / alzheimer disease / organophosphate / carbamylated / rivastigmine analogue / rational design |
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機能・相同性 | 機能・相同性情報
cholinesterase / cocaine metabolic process / neuroblast differentiation / Neurotransmitter clearance / cholinesterase activity / response to folic acid / choline binding / response to alkaloid / acetylcholine catabolic process / negative regulation of synaptic transmission ...cholinesterase / cocaine metabolic process / neuroblast differentiation / Neurotransmitter clearance / cholinesterase activity / response to folic acid / choline binding / response to alkaloid / acetylcholine catabolic process / negative regulation of synaptic transmission / peptide hormone processing / acetylcholinesterase activity / choline metabolic process / hydrolase activity, acting on ester bonds / nuclear envelope lumen / Aspirin ADME / Synthesis of PC / Synthesis, secretion, and deacylation of Ghrelin / catalytic activity / response to glucocorticoid / xenobiotic metabolic process / learning / amyloid-beta binding / blood microparticle / negative regulation of cell population proliferation / endoplasmic reticulum lumen / enzyme binding / extracellular space / extracellular region / identical protein binding / plasma membrane類似検索 - 分子機能 Acetylcholinesterase, tetramerisation domain / Acetylcholinesterase tetramerisation domain / Cholinesterase / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase type B, active site / Carboxylesterases type-B serine active site. / Carboxylesterase, type B / Carboxylesterase family / Alpha/Beta hydrolase fold, catalytic domain ...Acetylcholinesterase, tetramerisation domain / Acetylcholinesterase tetramerisation domain / Cholinesterase / Carboxylesterase type B, conserved site / Carboxylesterases type-B signature 2. / Carboxylesterase type B, active site / Carboxylesterases type-B serine active site. / Carboxylesterase, type B / Carboxylesterase family / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta類似検索 - ドメイン・相同性 |
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生物種 | Homo sapiens (ヒト) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.6 Å |
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データ登録者 | Brazzolotto, X. / De la Mora, E. / Dighe, S. / Ross, B. |
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引用 | ジャーナル: Commun Chem / 年: 2019 タイトル: Rivastigmine and metabolite analogues with putative Alzheimer's disease-modifying properties in a Caenorhabditis elegans model 著者: Dighe, S. / De la Mora, E. / Chan, S. / Kantham, S. / McColl, G. / Veliyath, S.K. / Miles, J.A. / Nessar, Z.Y. / Mcgeary, R. / Silman, I. / Weik, I. / Parat, M.O. / Brazzolotto, X. / Ross, B. |
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履歴 | 登録 | 2017年11月12日 | 登録サイト: PDBE / 処理サイト: PDBE |
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置き換え | 2018年11月21日 | ID: 6EUL |
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改定 1.0 | 2018年11月21日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2019年6月5日 | Group: Data collection / Database references / カテゴリ: citation / pdbx_database_proc Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year |
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改定 1.2 | 2020年7月29日 | Group: Data collection / Derived calculations / Structure summary カテゴリ: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_role 解説: Carbohydrate remediation / Provider: repository / タイプ: Remediation |
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改定 1.3 | 2024年1月17日 | Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary カテゴリ: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession |
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