登録情報 データベース : PDB / ID : 3lms 構造の表示 ダウンロードとリンクタイトル Structure of human activated thrombin-activatable fibrinolysis inhibitor, TAFIa, in complex with tick-derived funnelin inhibitor, TCI. 要素(Carboxypeptidase ...) x 2 詳細 キーワード HYDROLASE/HYDROLASE INHIBITOR / fibrinolysis / cogaulation / funnelin / alpha-beta-hydrolase / metallopeptidase / Alternative splicing / Carboxypeptidase / Disulfide bond / Glycoprotein / Hydrolase / Metal-binding / Metalloprotease / Polymorphism / Protease / Secreted / Zinc / Zymogen / Blood coagulation / Metalloenzyme inhibitor / Metalloprotease inhibitor / 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
carboxypeptidase U / positive regulation of extracellular matrix constituent secretion / acquisition of nutrients from host / negative regulation of hepatocyte proliferation / metalloendopeptidase inhibitor activity / negative regulation of plasminogen activation / enzyme inhibitor activity / negative regulation of fibrinolysis / Metabolism of Angiotensinogen to Angiotensins / metallocarboxypeptidase activity ... carboxypeptidase U / positive regulation of extracellular matrix constituent secretion / acquisition of nutrients from host / negative regulation of hepatocyte proliferation / metalloendopeptidase inhibitor activity / negative regulation of plasminogen activation / enzyme inhibitor activity / negative regulation of fibrinolysis / Metabolism of Angiotensinogen to Angiotensins / metallocarboxypeptidase activity / fibrinolysis / liver regeneration / Regulation of Complement cascade / cellular response to glucose stimulus / protein catabolic process / blood coagulation / toxin activity / response to xenobiotic stimulus / proteolysis / extracellular space / zinc ion binding / extracellular exosome / extracellular region 類似検索 - 分子機能 Carboxypeptidase inhibitor, N-terminal domain / Carboxypeptidase inhibitor I68 / Carboxypeptidase inhibitor I68 / Carboxypeptidase B2 / Anthopleurin-A / Myotoxin/Anemone neurotoxin domain superfamily / Anthopleurin-A / ligand-binding face of the semaphorins, domain 2 / Carboxypeptidase, activation peptide / Metallocarboxypeptidase-like, propeptide ... Carboxypeptidase inhibitor, N-terminal domain / Carboxypeptidase inhibitor I68 / Carboxypeptidase inhibitor I68 / Carboxypeptidase B2 / Anthopleurin-A / Myotoxin/Anemone neurotoxin domain superfamily / Anthopleurin-A / ligand-binding face of the semaphorins, domain 2 / Carboxypeptidase, activation peptide / Metallocarboxypeptidase-like, propeptide / Carboxypeptidase activation peptide / Peptidase family M14 domain profile. / Zn_pept / Peptidase M14, carboxypeptidase A / Zinc carboxypeptidase / Zn peptidases / Single Sheet / Aminopeptidase / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta 類似検索 - ドメイン・相同性 GLYCINE / : / Carboxypeptidase inhibitor / Carboxypeptidase B2 類似検索 - 構成要素生物種 Rhipicephalus bursa (ダニ)Homo sapiens (ヒト)手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 2.5 Å 詳細データ登録者 Sanglas, L. / Arolas, J.L. / Valnickova, Z. / Aviles, F.X. / Enghild, J.J. / Gomis-Ruth, F.X. 引用ジャーナル : J.Thromb.Haemost. / 年 : 2010タイトル : Insights into the molecular inactivation mechanism of human activated thrombin-activatable fibrinolysis inhibitor著者 : Sanglas, L. / Arolas, J.L. / Valnickova, Z. / Aviles, F.X. / Enghild, J.J. / Gomis-Ruth, F.X. 履歴 登録 2010年2月1日 登録サイト : RCSB / 処理サイト : PDBJ改定 1.0 2010年2月16日 Provider : repository / タイプ : Initial release改定 1.1 2011年7月13日 Group : Version format compliance改定 1.2 2017年11月1日 Group : Refinement description / カテゴリ : software / Item : _software.name改定 1.3 2023年11月1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 / pdbx_struct_conn_angle / struct_conn / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _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.ptnr3_auth_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.ptnr1_auth_asym_id / _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_asym_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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