登録情報 データベース : PDB / ID : 4jk5 構造の表示 ダウンロードとリンクタイトル Human urokinase-type Plasminogen Activator (uPA) in complex with a bicyclic peptide inhibitor (UK18-D-Ser) 要素Urokinase-type plasminogen activator bicyclic peptide UK18-D-Ser, uPA inhibitor 詳細キーワード HYDROLASE/HYDROLASE INHIBITOR / serine protease / chymotrypsin fold / urokinase-type plasminogen activator / bicyclic peptide inhibitor / D-amino acid / 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
u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity ... u-plasminogen activator / regulation of smooth muscle cell-matrix adhesion / urokinase plasminogen activator signaling pathway / regulation of plasminogen activation / regulation of fibrinolysis / regulation of wound healing / protein complex involved in cell-matrix adhesion / negative regulation of plasminogen activation / regulation of smooth muscle cell migration / regulation of signaling receptor activity / serine-type endopeptidase complex / Dissolution of Fibrin Clot / smooth muscle cell migration / plasminogen activation / regulation of cell adhesion mediated by integrin / tertiary granule membrane / negative regulation of fibrinolysis / regulation of cell adhesion / specific granule membrane / serine protease inhibitor complex / fibrinolysis / chemotaxis / blood coagulation / regulation of cell population proliferation / response to hypoxia / positive regulation of cell migration / external side of plasma membrane / serine-type endopeptidase activity / focal adhesion / Neutrophil degranulation / cell surface / signal transduction / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane 類似検索 - 分子機能 Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Kringle-like fold / EGF-like domain profile. / EGF-like domain signature 1. ... Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Kringle-like fold / EGF-like domain profile. / EGF-like domain signature 1. / EGF-like domain / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta 類似検索 - ドメイン・相同性 bicyclic peptide UK18-D-Ser / 1,3,5-tris(bromomethyl)benzene / Urokinase-type plasminogen activator 類似検索 - 構成要素生物種 Homo sapiens (ヒト)Synthetic construct (人工物) 手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 1.55 Å 詳細データ登録者 Buth, S.A. / Leiman, P.G. / Chen, S. / Heinis, C. 引用ジャーナル : Chembiochem / 年 : 2013タイトル : Improving binding affinity and stability of Peptide ligands by substituting glycines with d-amino acids.著者 : Chen, S. / Gfeller, D. / Buth, S.A. / Michielin, O. / Leiman, P.G. / Heinis, C. 履歴 登録 2013年3月9日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2013年7月17日 Provider : repository / タイプ : Initial release改定 1.1 2013年7月31日 Group : Database references改定 1.2 2017年11月15日 Group : Refinement description / カテゴリ : software改定 1.3 2021年6月2日 Group : Database references / Derived calculations / Source and taxonomyカテゴリ : entity_src_gen / struct_conn ... entity_src_gen / struct_conn / struct_ref_seq_dif / struct_site Item : _entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_host_org_cell_line ... _entity_src_gen.host_org_common_name / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_value_order / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_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 1.4 2023年9月20日 Group : Data collection / Database references / Refinement descriptionカテゴリ : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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