登録情報 | データベース: PDB / ID: 8raj |
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タイトル | NMR structure of PKS docking domains |
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要素 | - Beta-ketoacyl synthase
- Trimethylamine monooxygenase
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キーワード | PROTEIN BINDING / DOCKING DOMAIN / POLYKETIDE SYNTHASE |
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機能・相同性 | 機能・相同性情報
N,N-dimethylaniline monooxygenase activity / metabolic process / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / DIM/DIP cell wall layer assembly / secondary metabolite biosynthetic process / fatty acid synthase activity / transaminase activity / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity ...N,N-dimethylaniline monooxygenase activity / metabolic process / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / DIM/DIP cell wall layer assembly / secondary metabolite biosynthetic process / fatty acid synthase activity / transaminase activity / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / pyridoxal phosphate binding / NADP binding / flavin adenine dinucleotide binding / plasma membrane / cytoplasm類似検索 - 分子機能 Flavin monooxygenase FMO / Flavin monooxygenase-like / Flavin-binding monooxygenase-like / : / : / Polyketide synthase dehydratase domain / : / Polyketide and metazoan fatty acid synthase dehydratase (PKS/mFAS DH) domain profile. / PKS_PP_betabranch / Polyketide synthase dehydratase N-terminal domain ...Flavin monooxygenase FMO / Flavin monooxygenase-like / Flavin-binding monooxygenase-like / : / : / Polyketide synthase dehydratase domain / : / Polyketide and metazoan fatty acid synthase dehydratase (PKS/mFAS DH) domain profile. / PKS_PP_betabranch / Polyketide synthase dehydratase N-terminal domain / PKS_DH / Polyketide synthase, dehydratase domain / Polyketide synthase, dehydratase domain superfamily / Polyketide synthase, ketoreductase domain / KR domain / Aminotransferase class-III / Aminotransferase class-III / Polyketide synthase, C-terminal extension / Ketoacyl-synthetase C-terminal extension / PKS_KR / Ketosynthase family 3 (KS3) domain profile. / Polyketide synthase, phosphopantetheine-binding domain / Phosphopantetheine attachment site / Beta-ketoacyl synthase / Beta-ketoacyl synthase, active site / Ketosynthase family 3 (KS3) active site signature. / Polyketide synthase, beta-ketoacyl synthase domain / Beta-ketoacyl synthase, N-terminal / Beta-ketoacyl synthase, C-terminal / Beta-ketoacyl synthase, N-terminal domain / Beta-ketoacyl synthase, C-terminal domain / alpha/beta hydrolase fold / Alpha/beta hydrolase fold-1 / Thiolase-like / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / FAD/NAD(P)-binding domain superfamily / Alpha/Beta hydrolase fold / NAD(P)-binding domain superfamily類似検索 - ドメイン・相同性 Beta-ketoacyl synthase / Carrier domain-containing protein類似検索 - 構成要素 |
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生物種 | Methylorubrum extorquens AM1 (バクテリア) |
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手法 | 溶液NMR / simulated annealing |
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データ登録者 | Scat, S. / Weissman, K.J. / Chagot, B. |
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資金援助 | フランス, 1件 組織 | 認可番号 | 国 |
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Centre National de la Recherche Scientifique (CNRS) | | フランス |
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引用 | ジャーナル: Rsc Chem Biol / 年: 2024 タイトル: Insights into docking in megasynthases from the investigation of the toblerol trans -AT polyketide synthase: many alpha-helical means to an end. 著者: Scat, S. / Weissman, K.J. / Chagot, B. |
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履歴 | 登録 | 2023年12月1日 | 登録サイト: PDBE / 処理サイト: PDBE |
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改定 1.0 | 2024年6月5日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2024年7月17日 | Group: Database references / カテゴリ: citation / citation_author Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name |
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