登録情報 | データベース: PDB / ID: 1tiw |
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タイトル | Crystal structure of E. coli PutA proline dehydrogenase domain (residues 86-669) complexed with L-Tetrahydro-2-furoic acid |
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要素 | Bifunctional putA protein |
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キーワード | OXIDOREDUCTASE / beta/alpha barrel / flavoenzyme / FAD / proline catabolism |
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機能・相同性 | 機能・相同性情報
proline dehydrogenase / proline dehydrogenase activity / L-glutamate gamma-semialdehyde dehydrogenase / 1-pyrroline-5-carboxylate dehydrogenase activity / proline catabolic process to glutamate / proline biosynthetic process / DNA-binding transcription repressor activity / cis-regulatory region sequence-specific DNA binding / cytoplasmic side of plasma membrane / flavin adenine dinucleotide binding ...proline dehydrogenase / proline dehydrogenase activity / L-glutamate gamma-semialdehyde dehydrogenase / 1-pyrroline-5-carboxylate dehydrogenase activity / proline catabolic process to glutamate / proline biosynthetic process / DNA-binding transcription repressor activity / cis-regulatory region sequence-specific DNA binding / cytoplasmic side of plasma membrane / flavin adenine dinucleotide binding / response to oxidative stress / sequence-specific DNA binding / negative regulation of DNA-templated transcription / protein homodimerization activity / DNA binding / identical protein binding / plasma membrane / cytosol類似検索 - 分子機能 Single helix bin / : / PutA, RHH domain / TIM Barrel - #220 / Proline dehydrogenase PutA, domain I / Proline utilization A proline dehydrogenase N-terminal domain / Proline utilization A proline dehydrogenase N-terminal domain / Delta-1-pyrroline-5-carboxylate dehydrogenase 3 / Proline dehydrogenase PutA, domain II / Proline dehydrogenase PutA, domain I/II ...Single helix bin / : / PutA, RHH domain / TIM Barrel - #220 / Proline dehydrogenase PutA, domain I / Proline utilization A proline dehydrogenase N-terminal domain / Proline utilization A proline dehydrogenase N-terminal domain / Delta-1-pyrroline-5-carboxylate dehydrogenase 3 / Proline dehydrogenase PutA, domain II / Proline dehydrogenase PutA, domain I/II / DNA-binding domain of Proline dehydrogenase / Bifunctional protein PutA / Proline dehydrogenase domain / Proline dehydrogenase / FAD-linked oxidoreductase-like / Arc-type ribbon-helix-helix / Ribbon-helix-helix / Aldehyde dehydrogenase, glutamic acid active site / Aldehyde dehydrogenases glutamic acid active site. / Aldehyde dehydrogenase, cysteine active site / Aldehyde dehydrogenases cysteine active site. / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, N-terminal / Aldehyde dehydrogenase, C-terminal / Aldehyde/histidinol dehydrogenase / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / TIM Barrel / Alpha-Beta Barrel / Up-down Bundle / Mainly Alpha / Alpha Beta類似検索 - ドメイン・相同性 FLAVIN-ADENINE DINUCLEOTIDE / TETRAHYDROFURAN-2-CARBOXYLIC ACID / Bifunctional protein PutA類似検索 - 構成要素 |
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生物種 | ![](img/tx_bacteria.gif) Escherichia coli (大腸菌) |
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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 Å |
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データ登録者 | Tanner, J.J. / Zhang, M. / White, T.A. / Schuermann, J.P. / Baban, B.A. / Becker, D.F. |
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引用 | ジャーナル: Biochemistry / 年: 2004 タイトル: Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors 著者: Zhang, M. / White, T.A. / Schuermann, J.P. / Baban, B.A. / Becker, D.F. / Tanner, J.J. |
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履歴 | 登録 | 2004年6月2日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2004年10月26日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2008年4月30日 | Group: Version format compliance |
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改定 1.2 | 2011年7月13日 | Group: Advisory / Version format compliance |
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改定 1.3 | 2023年8月23日 | Group: Data collection / Database references ...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 / 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 / _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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