登録情報 データベース : PDB / ID : 1tt5 構造の表示 ダウンロードとリンクタイトル Structure of APPBP1-UBA3-Ubc12N26: a unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8 要素Ubiquitin-conjugating enzyme E2 M amyloid protein-binding protein 1 アミロイド ubiquitin-activating enzyme E1C isoform 1 詳細キーワード CELL CYCLE (細胞周期) / LIGASE (リガーゼ)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
E2 NEDD8-conjugating enzyme / NEDD8 conjugating enzyme activity / E1 NEDD8-activating enzyme / NEDD8 activating enzyme activity / endomitotic cell cycle / ubiquitin activating enzyme activity / NEDD8 transferase activity / mitotic DNA replication checkpoint signaling / protein neddylation / TGF-beta receptor signaling activates SMADs ... E2 NEDD8-conjugating enzyme / NEDD8 conjugating enzyme activity / E1 NEDD8-activating enzyme / NEDD8 activating enzyme activity / endomitotic cell cycle / ubiquitin activating enzyme activity / NEDD8 transferase activity / mitotic DNA replication checkpoint signaling / protein neddylation / TGF-beta receptor signaling activates SMADs / regulation of neuron apoptotic process / post-translational protein modification / NIK-->noncanonical NF-kB signaling / Dectin-1 mediated noncanonical NF-kB signaling / protein modification process / ubiquitin-protein transferase activity / positive regulation of neuron apoptotic process / Antigen processing: Ubiquitination & Proteasome degradation / Neddylation / ubiquitin-dependent protein catabolic process / neuron apoptotic process / regulation of apoptotic process / protein ubiquitination / regulation of cell cycle / protein heterodimerization activity / DNA damage response / ubiquitin protein ligase binding / シグナル伝達 / protein-containing complex / タンパク質分解 / 核質 / ATP binding / identical protein binding / 細胞核 / 細胞膜 / 細胞質基質 / 細胞質 類似検索 - 分子機能 NEDD8-activating enzyme E1, catalytic subunit / NEDD8-activating enzyme E1 regulatory subunit APP-BP1 / E2 binding / NEDD8-activating enzyme E1 catalytic subunit / E2 binding domain / E2_bind / Ubiquitin activating enzymes (Uba3). Chain: B, domain 2 / Ubiquitin activating enzyme, alpha domain superfamily / Ubiquitin-activating enzyme E1, Cys active site / Ubiquitin-activating enzyme active site. ... NEDD8-activating enzyme E1, catalytic subunit / NEDD8-activating enzyme E1 regulatory subunit APP-BP1 / E2 binding / NEDD8-activating enzyme E1 catalytic subunit / E2 binding domain / E2_bind / Ubiquitin activating enzymes (Uba3). Chain: B, domain 2 / Ubiquitin activating enzyme, alpha domain superfamily / Ubiquitin-activating enzyme E1, Cys active site / Ubiquitin-activating enzyme active site. / ThiF/MoeB/HesA family / ユビキチン活性化酵素 / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / ユビキチン結合酵素 / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / Ubiquitin-like (UB roll) / Arc Repressor Mutant, subunit A / NAD(P)-binding Rossmann-like Domain / Roll / ロスマンフォールド / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta 類似検索 - ドメイン・相同性 : / : / NEDD8-conjugating enzyme Ubc12 / NEDD8-activating enzyme E1 regulatory subunit / NEDD8-activating enzyme E1 catalytic subunit 類似検索 - 構成要素生物種 Homo sapiens (ヒト)手法 X線回折 / シンクロトロン / 分子置換 / 解像度 : 2.6 Å 詳細データ登録者 Huang, D.T. / Miller, D.W. / Mathew, R. / Cassell, R. / Holton, J.M. / Roussel, M.F. / Schulman, B.A. 引用ジャーナル : Nat.Struct.Mol.Biol. / 年 : 2004タイトル : A unique E1-E2 interaction required for optimal conjugation of the ubiquitin-like protein NEDD8.著者 : Huang, D.T. / Miller, D.W. / Mathew, R. / Cassell, R. / Holton, J.M. / Roussel, M.F. / Schulman, B.A. 履歴 登録 2004年6月21日 登録サイト : RCSB / 処理サイト : RCSB改定 1.0 2004年9月14日 Provider : repository / タイプ : Initial release改定 1.1 2008年4月30日 Group : Version format compliance改定 1.2 2011年7月13日 Group : Version format compliance改定 1.3 2024年2月14日 Group : Data collection / Database references / Derived calculationsカテゴリ : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / 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_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_ref_seq_dif.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 Residue B SER 608 and Residue B VAL 701 are not linked. Distance of C-N bond is 6.15. ... SEQUENCE Residue B SER 608 and Residue B VAL 701 are not linked. Distance of C-N bond is 6.15. Residue B THR 384 and Residue B ASN 601 are linked together. The residues 600-1008 of chains B and D were modelled as alanines due to poor electron density. The residue names were assigned arbitrarily as there are multiple possible sequences consistent with the density, and the connectivity is unclear.