登録情報 | データベース: PDB / ID: 6nya |
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タイトル | Crystal Structure of ubiquitin E1 (Uba1) in complex with Ubc3 (Cdc34) and ubiquitin |
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要素 | - Ubiquitin
- Ubiquitin-activating enzyme E1 1
- Ubiquitin-conjugating enzyme E2-34 kDa
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キーワード | LIGASE/TRANSFERASE / CONFORMATIONAL CHANGE / THIOESTER / ADENYLATION / THIOESTER TRANSFER / TRANSTHIOESTERIFICATION / ATP-BINDING / UBIQUITIN E2-BINDING / UBIQUITINATION / LIGASE / LIGASE-TRANSFERASE complex |
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機能・相同性 | 機能・相同性情報
regulation of transcription by galactose / regulation of sulfur amino acid metabolic process / cellular response to methylmercury / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / positive regulation of D-glucose transmembrane transport / mitotic intra-S DNA damage checkpoint signaling / mitochondrial fusion / regulation of metabolic process ...regulation of transcription by galactose / regulation of sulfur amino acid metabolic process / cellular response to methylmercury / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / positive regulation of D-glucose transmembrane transport / mitotic intra-S DNA damage checkpoint signaling / mitochondrial fusion / regulation of metabolic process / silent mating-type cassette heterochromatin formation / SCF ubiquitin ligase complex / E2 ubiquitin-conjugating enzyme / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / ubiquitin conjugating enzyme activity / Antigen processing: Ubiquitination & Proteasome degradation / subtelomeric heterochromatin formation / protein autoubiquitination / regulation of mitotic cell cycle / G1/S transition of mitotic cell cycle / protein polyubiquitination / ubiquitin-protein transferase activity / G2/M transition of mitotic cell cycle / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / chromosome, telomeric region / DNA replication / protein ubiquitination / cell division / mRNA binding / DNA damage response / ATP binding / nucleus / cytoplasm類似検索 - 分子機能 Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2 / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, UFD domain / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, conserved site / Ubiquitin-activating enzyme signature 1. / Ubiquitin-activating enzyme E1 / Ubiquitin-activating enzyme E1, C-terminal / Ubiquitin-activating enzyme E1, FCCH domain ...Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2 / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, UFD domain / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, conserved site / Ubiquitin-activating enzyme signature 1. / Ubiquitin-activating enzyme E1 / Ubiquitin-activating enzyme E1, C-terminal / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, four-helix bundle / Ubiquitin-activating enzyme E1, C-terminal domain superfamily / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, FCCH domain superfamily / Ubiquitin fold domain / Ubiquitin-activating enzyme E1 FCCH domain / Ubiquitin-activating enzyme E1 four-helix bundle / Ubiquitin-activating enzyme e1 C-terminal domain / Ubiquitin-activating enzyme, SCCH domain / Ubiquitin-activating enzyme, SCCH domain / Ubiquitin/SUMO-activating enzyme E1-like / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, Cys active site / Ubiquitin-activating enzyme active site. / ThiF/MoeB/HesA family / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin-activating enzyme / Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A / : / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / Elongation Factor Tu (Ef-tu); domain 3 / FAD/NAD(P)-binding domain / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / 3-Layer(bba) Sandwich / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Arc Repressor Mutant, subunit A / NAD(P)-binding Rossmann-like Domain / Ubiquitin-like domain superfamily / Roll / Beta Barrel / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta類似検索 - ドメイン・相同性 ADENOSINE-5'-TRIPHOSPHATE / Ubiquitin-like domain-containing protein / Ubiquitin-conjugating enzyme E2-34 kDa / Ubiquitin-activating enzyme E1 1 / Ubiquitin類似検索 - 構成要素 |
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生物種 |  Saccharomyces cerevisiae (パン酵母)
 Triticum aestivum (コムギ) |
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手法 | X線回折 / シンクロトロン / 分子置換 / 解像度: 2.065 Å |
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データ登録者 | Olsen, S.K. / Williams, K.M. / Atkison, J.H. |
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資金援助 | 米国, 1件 組織 | 認可番号 | 国 |
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National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | GM115568 | 米国 |
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引用 | ジャーナル: Nat Commun / 年: 2019 タイトル: Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34. 著者: Williams, K.M. / Qie, S. / Atkison, J.H. / Salazar-Arango, S. / Alan Diehl, J. / Olsen, S.K. |
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履歴 | 登録 | 2019年2月11日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2019年8月7日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2020年1月1日 | Group: Author supporting evidence / カテゴリ: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization |
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改定 1.2 | 2023年10月11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 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_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.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.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 |
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改定 1.3 | 2024年10月30日 | Group: Structure summary カテゴリ: pdbx_entry_details / pdbx_modification_feature |
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