Entry | Database: PDB / ID: 6zhu |
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Title | Yeast Uba1 in complex with Ubc3 and ATP |
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Components | - Ubiquitin-activating enzyme E1 1
- Ubiquitin-conjugating enzyme E2-34 kDa
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Keywords | LIGASE / Ubiquitin / E1 / Ubc3 / Cdc34 |
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Function / homology | Function and homology information
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 / Antigen processing: Ubiquitination & Proteasome degradation / regulation of metabolic process / positive regulation of glucose transmembrane transport / mitotic intra-S DNA damage checkpoint signaling ...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 / Antigen processing: Ubiquitination & Proteasome degradation / regulation of metabolic process / positive regulation of glucose transmembrane transport / mitotic intra-S DNA damage checkpoint signaling / mitochondrial fusion / 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 / 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 / DNA replication / chromosome, telomeric region / protein ubiquitination / cell division / DNA damage response / ATP binding / nucleus / cytoplasmSimilarity search - Function 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, 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 / Ubiquitin-activating enzyme / 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 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-likeSimilarity search - Domain/homology |
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Biological species | ![](img/tx_yeast.gif) ![](data/taxo/icon/Saccharomyces_cerevisiae_S.png) Saccharomyces cerevisiae (brewer's yeast) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.18 Å |
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Authors | Misra, M. / Schindelin, H. |
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Funding support | Germany, 1items Organization | Grant number | Country |
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German Research Foundation (DFG) | SCHI 425-6/1 | Germany |
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Citation | Journal: To Be Published Title: ATP induced conformational changes facilitate E1-E2 disulfide bridging in the ubiquitin system Authors: Misra, M. / Schaefer, A. / Kuhn, M. / Pluska, L. / Tessmer, I. / Sommer, T. / Schindelin, H. |
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History | Deposition | Jun 23, 2020 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Jan 12, 2022 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jan 24, 2024 | Group: Data collection / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id |
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