登録情報 データベース : PDB / ID : 2wnp 構造の表示 ダウンロードとリンクタイトル M-ficolin mutant Y271F 要素FICOLIN-1 詳細 キーワード IMMUNE SYSTEM / GLYCOPROTEIN / INNATE IMMUNITY / FIBRINOGEN-LIKE DOMAIN / CARBOHYDRATE RECOGNITION / LECTIN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
recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / cell surface pattern recognition receptor signaling pathway / complement activation, lectin pathway / sialic acid binding / negative regulation of viral entry into host cell / carbohydrate derivative binding / collagen trimer ... recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / cell surface pattern recognition receptor signaling pathway / complement activation, lectin pathway / sialic acid binding / negative regulation of viral entry into host cell / carbohydrate derivative binding / collagen trimer / protein localization to cell surface / serine-type endopeptidase complex / pattern recognition receptor activity / Initial triggering of complement / positive regulation of interleukin-8 production / G protein-coupled receptor binding / antigen binding / carbohydrate binding / secretory granule lumen / collagen-containing extracellular matrix / ficolin-1-rich granule lumen / G protein-coupled receptor signaling pathway / external side of plasma membrane / signaling receptor binding / Neutrophil degranulation / proteolysis / extracellular space / extracellular region / metal ion binding / plasma membrane 類似検索 - 分子機能 Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2 / Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2 / Gamma Fibrinogen; Chain A, domain 1 / Gamma Fibrinogen, chain A, domain 1 / Fibrinogen, conserved site / Fibrinogen C-terminal domain signature. / Fibrinogen-related domains (FReDs) / Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 / Fibrinogen beta and gamma chains, C-terminal globular domain / Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain ... Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2 / Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2 / Gamma Fibrinogen; Chain A, domain 1 / Gamma Fibrinogen, chain A, domain 1 / Fibrinogen, conserved site / Fibrinogen C-terminal domain signature. / Fibrinogen-related domains (FReDs) / Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 / Fibrinogen beta and gamma chains, C-terminal globular domain / Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain / Fibrinogen-like, C-terminal / Fibrinogen C-terminal domain profile. / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / Few Secondary Structures / Irregular / 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 / シンクロトロン / 分子置換 / 解像度 : 1.21 Å 詳細データ登録者 Gout, E. / Garlatti, V. / Smith, D.F. / Lacroix, M. / Dumestre-Perard, C. / Lunardi, T. / Arlaud, G.J. / Gaboriaud, C. / Thielens, N.M. 引用ジャーナル : J.Biol.Chem. / 年 : 2010タイトル : Carbohydrate Recognition Properties of Human Ficolins: Glycan Array Screening Reveals the Sialic Acid Binding Specificity of M-Ficolin.著者 : Gout, E. / Garlatti, V. / Smith, D.F. / Lacroix, M. / Dumestre-Perard, C. / Lunardi, T. / Martin, L. / Cesbron, J.Y. / Arlaud, G.J. / Gaboriaud, C. / Thielens, N.M. 履歴 登録 2009年7月16日 登録サイト : PDBE / 処理サイト : PDBE改定 1.0 2009年12月22日 Provider : repository / タイプ : Initial release改定 1.1 2011年5月8日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Version format compliance改定 1.3 2023年12月13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 / 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_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_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_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 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.