Entry | Database: PDB / ID: 6h77 |
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Title | E1 enzyme for ubiquitin like protein activation in complex with UBL |
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Components | - Ubiquitin-fold modifier 1
- Ubiquitin-like modifier-activating enzyme 5
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Keywords | SIGNALING PROTEIN / Ubiquitin like protein activating enzyme |
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Function / homology | Function and homology information
UFM1 activating enzyme activity / protein ufmylation / protein K69-linked ufmylation / megakaryocyte differentiation / regulation of intracellular estrogen receptor signaling pathway / reticulophagy / neuromuscular process / negative regulation of protein import into nucleus / response to endoplasmic reticulum stress / erythrocyte differentiation ...UFM1 activating enzyme activity / protein ufmylation / protein K69-linked ufmylation / megakaryocyte differentiation / regulation of intracellular estrogen receptor signaling pathway / reticulophagy / neuromuscular process / negative regulation of protein import into nucleus / response to endoplasmic reticulum stress / erythrocyte differentiation / brain development / Antigen processing: Ubiquitination & Proteasome degradation / intracellular membrane-bounded organelle / endoplasmic reticulum membrane / negative regulation of apoptotic process / Golgi apparatus / endoplasmic reticulum / protein homodimerization activity / zinc ion binding / ATP binding / nucleus / cytoplasm / cytosolSimilarity search - Function Ubiquitin-fold modifier 1 / Ubiquitin fold modifier 1 protein / D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site 1 / ThiF/MoeB/HesA family / Ubiquitin-activating enzyme / THIF-type NAD/FAD binding fold / ThiF family / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin-like domain superfamily ...Ubiquitin-fold modifier 1 / Ubiquitin fold modifier 1 protein / D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding domain conserved site 1 / ThiF/MoeB/HesA family / Ubiquitin-activating enzyme / THIF-type NAD/FAD binding fold / ThiF family / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin-like domain superfamily / Roll / Alpha BetaSimilarity search - Domain/homology ADENOSINE-5'-TRIPHOSPHATE / DI(HYDROXYETHYL)ETHER / Ubiquitin-fold modifier 1 / Ubiquitin-like modifier-activating enzyme 5Similarity search - Component |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å |
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Authors | Soudah, N. / Padala, P. / Hassouna, F. / Mashahreh, B. / Lebedev, A.A. / Isupov, M.N. / Cohen-Kfir, E. / Wiener, R. |
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Citation | Journal: J.Mol.Biol. / Year: 2019 Title: An N-Terminal Extension to UBA5 Adenylation Domain Boosts UFM1 Activation: Isoform-Specific Differences in Ubiquitin-like Protein Activation. Authors: Soudah, N. / Padala, P. / Hassouna, F. / Kumar, M. / Mashahreh, B. / Lebedev, A.A. / Isupov, M.N. / Cohen-Kfir, E. / Wiener, R. |
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History | Deposition | Jul 30, 2018 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Oct 31, 2018 | Provider: repository / Type: Initial release |
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Revision 1.1 | Apr 24, 2019 | Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year |
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Revision 1.2 | Jan 17, 2024 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim 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.ptnr3_auth_seq_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 / _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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