登録情報 | データベース: PDB / ID: 6had |
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タイトル | Human transketolase variant E160Q |
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要素 | Transketolase |
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キーワード | TRANSFERASE / THIAMIN DIPHOSPHATE / TPP / THDP / ENZYME / CATALYSIS / SUGAR METABOLISM |
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機能・相同性 | 機能・相同性情報
xylulose 5-phosphate biosynthetic process / Insulin effects increased synthesis of Xylulose-5-Phosphate / Pentose phosphate pathway / transketolase / transketolase activity / pentose-phosphate shunt, non-oxidative branch / pentose-phosphate shunt / NFE2L2 regulates pentose phosphate pathway genes / glyceraldehyde-3-phosphate biosynthetic process / regulation of growth ...xylulose 5-phosphate biosynthetic process / Insulin effects increased synthesis of Xylulose-5-Phosphate / Pentose phosphate pathway / transketolase / transketolase activity / pentose-phosphate shunt, non-oxidative branch / pentose-phosphate shunt / NFE2L2 regulates pentose phosphate pathway genes / glyceraldehyde-3-phosphate biosynthetic process / regulation of growth / thiamine pyrophosphate binding / peroxisome / vesicle / nuclear body / calcium ion binding / endoplasmic reticulum membrane / magnesium ion binding / protein homodimerization activity / extracellular exosome / nucleoplasm / cytosol類似検索 - 分子機能 : / Transketolase signature 1. / Transketolase, thiamine diphosphate binding domain / Transketolase binding site / Transketolase signature 2. / Transketolase, N-terminal / Transketolase, C-terminal domain / Transketolase, C-terminal domain / Rossmann fold - #920 / Transketolase-like, pyrimidine-binding domain ...: / Transketolase signature 1. / Transketolase, thiamine diphosphate binding domain / Transketolase binding site / Transketolase signature 2. / Transketolase, N-terminal / Transketolase, C-terminal domain / Transketolase, C-terminal domain / Rossmann fold - #920 / Transketolase-like, pyrimidine-binding domain / Transketolase, pyrimidine binding domain / Transketolase, pyrimidine binding domain / Transketolase C-terminal/Pyruvate-ferredoxin oxidoreductase domain II / Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains / Thiamin diphosphate-binding 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 / 解像度: 1.04 Å |
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データ登録者 | Dai, S. / Sautner, V. / Tittmann, K. |
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資金援助 | ドイツ, 1件 組織 | 認可番号 | 国 |
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German Research Foundation | FOR 1296/TP3 | ドイツ |
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引用 | ジャーナル: Nature / 年: 2019 タイトル: Low-barrier hydrogen bonds in enzyme cooperativity. 著者: Dai, S. / Funk, L.M. / von Pappenheim, F.R. / Sautner, V. / Paulikat, M. / Schroder, B. / Uranga, J. / Mata, R.A. / Tittmann, K. |
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履歴 | 登録 | 2018年8月7日 | 登録サイト: PDBE / 処理サイト: PDBE |
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改定 1.0 | 2019年8月21日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2019年9月18日 | Group: Data collection / Database references / カテゴリ: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _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 | 2019年10月2日 | Group: Data collection / Database references / カテゴリ: citation / citation_author Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name |
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改定 1.3 | 2019年10月9日 | Group: Data collection / Database references / カテゴリ: citation Item: _citation.journal_volume / _citation.page_first / _citation.page_last |
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改定 2.0 | 2021年8月4日 | Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary カテゴリ: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_site.details / _struct_site.pdbx_auth_comp_id / _struct_site_gen.auth_comp_id / _struct_site_gen.label_comp_id |
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改定 2.1 | 2024年5月15日 | Group: Data collection / Database references / カテゴリ: chem_comp_atom / chem_comp_bond / database_2 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession |
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