登録情報 データベース : PDB / ID : 2ygf 構造の表示 ダウンロードとリンクタイトル L89V, L93I and V136M Mutant of N-Term HSP90 complexed with Geldanamycin 要素ATP-DEPENDENT MOLECULAR CHAPERONE HSP82 詳細 キーワード CHAPERONE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
The NLRP3 inflammasome / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1-dependent transactivation / HSF1 activation / response to oxygen levels / protein targeting to mitochondrion ... The NLRP3 inflammasome / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / eNOS activation / Extra-nuclear estrogen signaling / VEGFR2 mediated vascular permeability / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / HSF1-dependent transactivation / HSF1 activation / response to oxygen levels / protein targeting to mitochondrion / box C/D snoRNP assembly / regulation of telomere maintenance / response to osmotic stress / 'de novo' protein folding / protein maturation / proteasome assembly / Neutrophil degranulation / positive regulation of telomere maintenance via telomerase / ATP-dependent protein folding chaperone / disordered domain specific binding / unfolded protein binding / protein folding / cellular response to heat / protein refolding / protein stabilization / perinuclear region of cytoplasm / ATP hydrolysis activity / protein-containing complex / ATP binding / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol 類似検索 - 分子機能 Heat shock protein Hsp90, conserved site / Heat shock hsp90 proteins family signature. / HSP90, C-terminal domain / Heat shock protein Hsp90, N-terminal / Heat shock protein Hsp90 family / Hsp90 protein / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPase, C-terminal domain / Heat Shock Protein 90 / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase ... Heat shock protein Hsp90, conserved site / Heat shock hsp90 proteins family signature. / HSP90, C-terminal domain / Heat shock protein Hsp90, N-terminal / Heat shock protein Hsp90 family / Hsp90 protein / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPase, C-terminal domain / Heat Shock Protein 90 / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold / 2-Layer Sandwich / Alpha Beta 類似検索 - ドメイン・相同性 GELDANAMYCIN / ATP-dependent molecular chaperone HSP82 類似検索 - 構成要素生物種 SACCHAROMYCES CEREVISIAE (パン酵母)手法 X線回折 / 分子置換 / 解像度 : 2 Å 詳細データ登録者 Roe, M. / Prodromou, C. / Pearl, L.H. 引用ジャーナル : Faseb J. / 年 : 2011タイトル : Features of the Streptomyces Hygroscopicus Htpg Reveal How Partial Geldanamycin Resistance Can Arise by Mutation to the ATP Binding Pocket of a Eukaryotic Hsp90.著者 : Millson, S.H. / Chua, C.S. / Solovieva, S. / Roe, M. / Polier, S. / Pearl, L.H. / Sim, T.S. / Prodromou, C. / Piper, P.W. 履歴 登録 2011年4月14日 登録サイト : PDBE / 処理サイト : PDBE改定 1.0 2011年11月16日 Provider : repository / タイプ : Initial release改定 1.1 2012年3月21日 Group : Other改定 1.2 2013年2月6日 Group : Atomic model改定 2.0 2017年6月28日 Group : Advisory / Atomic model / Data collectionカテゴリ : atom_site / database_PDB_caveat / diffrn_sourceItem : _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.label_atom_id / _diffrn_source.type 改定 2.1 2024年5月1日 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description カテゴリ : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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