Entry | Database: PDB / ID: 6now |
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Title | Human Mitochondrial Alanyl-tRNA Synthetase C-Ala domain |
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Components | Alanine--tRNA ligase, mitochondrial |
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Keywords | LIGASE / Alanyl-tRNA synthetase / mitochondria / C-terminal domain / alpha-beta domain |
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Function / homology | Function and homology information
mitochondrial alanyl-tRNA aminoacylation / alanine-tRNA ligase / alanine-tRNA ligase activity / alanyl-tRNA aminoacylation / Mitochondrial tRNA aminoacylation / aminoacyl-tRNA editing activity / tRNA binding / mitochondrion / zinc ion binding / ATP bindingSimilarity search - Function Alanine-tRNA ligase, eukaryota/bacteria / Alanine-tRNA ligase, class IIc / Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily / Alanyl-tRNA synthetase, class IIc, N-terminal / Alanyl-tRNA synthetase, class IIc, core domain / tRNA synthetases class II (A) / Alanyl-transfer RNA synthetases family profile. / Threonyl/alanyl tRNA synthetase, SAD / Threonyl and Alanyl tRNA synthetase second additional domain / Threonyl and Alanyl tRNA synthetase second additional domain ...Alanine-tRNA ligase, eukaryota/bacteria / Alanine-tRNA ligase, class IIc / Alanine-tRNA ligase, class IIc, anti-codon-binding domain superfamily / Alanyl-tRNA synthetase, class IIc, N-terminal / Alanyl-tRNA synthetase, class IIc, core domain / tRNA synthetases class II (A) / Alanyl-transfer RNA synthetases family profile. / Threonyl/alanyl tRNA synthetase, SAD / Threonyl and Alanyl tRNA synthetase second additional domain / Threonyl and Alanyl tRNA synthetase second additional domain / Threonyl/alanyl tRNA synthetase, class II-like, putative editing domain superfamily / Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL) / Translation protein, beta-barrel domain superfamilySimilarity search - Domain/homology |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 4.099 Å |
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Authors | Kuhle, B. / Schimmel, P. |
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Citation | Journal: Nat Commun / Year: 2020 Title: Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs. Authors: Kuhle, B. / Chihade, J. / Schimmel, P. |
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History | Deposition | Jan 16, 2019 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Jan 22, 2020 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jul 29, 2020 | Group: Database references / Structure summary / Category: citation / citation_author / struct Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _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 / _citation_author.identifier_ORCID / _struct.title |
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Revision 1.2 | Oct 11, 2023 | Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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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