登録情報 データベース : PDB / ID : 1zcm 構造の表示 ダウンロードとリンクタイトル Human calpain protease core inhibited by ZLLYCH2F 要素Calpain 1, large [catalytic] subunit 詳細 キーワード HYDROLASE / Calcium binding / Protease / Thiol protease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
calpain-1 / calpain complex / mammary gland involution / calcium-dependent cysteine-type endopeptidase activity / receptor catabolic process / Formation of the cornified envelope / self proteolysis / cornified envelope / regulation of catalytic activity / regulation of NMDA receptor activity ... calpain-1 / calpain complex / mammary gland involution / calcium-dependent cysteine-type endopeptidase activity / receptor catabolic process / Formation of the cornified envelope / self proteolysis / cornified envelope / regulation of catalytic activity / regulation of NMDA receptor activity / Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models / regulation of macroautophagy / Degradation of the extracellular matrix / peptidase activity / ficolin-1-rich granule lumen / lysosome / focal adhesion / calcium ion binding / positive regulation of cell population proliferation / Neutrophil degranulation / mitochondrion / proteolysis / extracellular exosome / extracellular region / membrane / plasma membrane / cytoplasm / cytosol 類似検索 - 分子機能 Calpain subdomain III / Peptidase C2, calpain, domain III / calpain_III / Peptidase C2, calpain, large subunit, domain III / Peptidase C2, calpain family / Calpain large subunit, domain III superfamily / Calpain large subunit, domain III / Peptidase C2, calpain, catalytic domain / Calpain family cysteine protease / Cysteine proteinase, calpain-type, catalytic domain profile. ... Calpain subdomain III / Peptidase C2, calpain, domain III / calpain_III / Peptidase C2, calpain, large subunit, domain III / Peptidase C2, calpain family / Calpain large subunit, domain III superfamily / Calpain large subunit, domain III / Peptidase C2, calpain, catalytic domain / Calpain family cysteine protease / Cysteine proteinase, calpain-type, catalytic domain profile. / Calpain-like thiol protease family. / EF-hand domain pair / Cysteine proteinases / Cysteine peptidase, cysteine active site / Eukaryotic thiol (cysteine) proteases cysteine active site. / Cathepsin B; Chain A / Papain-like cysteine peptidase superfamily / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / Alpha-Beta Complex / Alpha Beta 類似検索 - ドメイン・相同性生物種 Homo sapiens (ヒト)手法 X線回折 / 分子置換 / 解像度 : 2 Å 詳細データ登録者 Li, Q. / Hanzlik, R.P. / Weaver, R.F. / Schonbrunn, E. 引用ジャーナル : Biochemistry / 年 : 2006タイトル : Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core著者 : Li, Q. / Hanzlik, R.P. / Weaver, R.F. / Schonbrunn, E. 履歴 登録 2005年4月12日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2006年1月31日 Provider : repository / タイプ : Initial release改定 1.1 2008年4月1日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Version format compliance改定 1.3 2017年10月11日 Group : Refinement description / カテゴリ : software改定 1.4 2021年10月20日 Group : Advisory / Database references / Derived calculationsカテゴリ : database_2 / pdbx_database_remark ... database_2 / pdbx_database_remark / pdbx_struct_conn_angle / struct_conn / 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 / _pdbx_database_remark.text / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id 改定 1.5 2023年8月23日 Group : Data collection / Refinement descriptionカテゴリ : chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
すべて表示 表示を減らす Remark 600 HETEROGEN As suggested by authors, the fluorine atom is detached from the ligand as a result of ... HETEROGEN As suggested by authors, the fluorine atom is detached from the ligand as a result of the chemical reaction involving modification of Cys 115.