登録情報 データベース : PDB / ID : 1sp4 構造の表示 ダウンロードとリンクタイトル Crystal structure of NS-134 in complex with bovine cathepsin B: a two headed epoxysuccinyl inhibitor extends along the whole active site cleft 要素(Cathepsin B) x 2 詳細 キーワード HYDROLASE/HYDROLASE INHIBITOR / cathepsin B / epoxysuccinyl-based inhibitors / inhibitor design / HYDROLASE / HYDROLASE-HYDROLASE INHIBITOR complex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
Trafficking and processing of endosomal TLR / Collagen degradation / cathepsin B / MHC class II antigen presentation / Neutrophil degranulation / proteolysis involved in protein catabolic process / melanosome / endopeptidase activity / lysosome / apical plasma membrane ... Trafficking and processing of endosomal TLR / Collagen degradation / cathepsin B / MHC class II antigen presentation / Neutrophil degranulation / proteolysis involved in protein catabolic process / melanosome / endopeptidase activity / lysosome / apical plasma membrane / cysteine-type endopeptidase activity / extracellular space 類似検索 - 分子機能 Peptidase C1A, propeptide / Peptidase family C1 propeptide / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / : / Cysteine peptidase, asparagine active site / Eukaryotic thiol (cysteine) proteases asparagine active site. / Cysteine peptidase, histidine active site / Eukaryotic thiol (cysteine) proteases histidine active site. / Peptidase C1A, papain C-terminal / Papain family cysteine protease ... Peptidase C1A, propeptide / Peptidase family C1 propeptide / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / : / Cysteine peptidase, asparagine active site / Eukaryotic thiol (cysteine) proteases asparagine active site. / Cysteine peptidase, histidine active site / Eukaryotic thiol (cysteine) proteases histidine active site. / Peptidase C1A, papain C-terminal / Papain family cysteine protease / Papain family cysteine protease / Cysteine proteinases / Cysteine peptidase, cysteine active site / Eukaryotic thiol (cysteine) proteases cysteine active site. / Cathepsin B; Chain A / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Papain-like cysteine peptidase superfamily / Alpha-Beta Complex / Up-down Bundle / Mainly Alpha / Alpha Beta 類似検索 - ドメイン・相同性 NS-134 TWO HEADED EPOXYSUCCINYL INHIBITOR / Chem-EP2 / Cathepsin B 類似検索 - 構成要素生物種 Bos taurus (ウシ)手法 X線回折 / 分子置換 / 解像度 : 2.2 Å 詳細データ登録者 Stern, I. / Schaschke, N. / Moroder, L. / Turk, D. 引用ジャーナル : Biochem.J. / 年 : 2004タイトル : Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft.著者 : Stern, I. / Schaschke, N. / Moroder, L. / Turk, D. 履歴 登録 2004年3月16日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2004年5月4日 Provider : repository / タイプ : Initial release改定 1.1 2008年4月29日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Atomic model / Database references ... Atomic model / Database references / Derived calculations / Non-polymer description / Structure summary / Version format compliance 改定 1.3 2012年12月12日 Group : Other改定 1.4 2014年2月12日 Group : Refinement description改定 1.5 2017年10月11日 Group : Advisory / Refinement descriptionカテゴリ : pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / softwareItem : _software.classification / _software.name改定 1.6 2024年3月13日 Group : Advisory / Data collection ... Advisory / Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary カテゴリ : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_entity_src_syn / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
すべて表示 表示を減らす Remark 999 SEQUENCE THE PROTEIN IS POSTRANSLATIONALLY MODIFIED. AFTER THE ENZYME IS PROCESSED, THE PEPTIDE ... SEQUENCE THE PROTEIN IS POSTRANSLATIONALLY MODIFIED. AFTER THE ENZYME IS PROCESSED, THE PEPTIDE BOND BETWEEN THE RESIDUES 48 49 IS CLEAVED.