Entry | Database: PDB / ID: 3r8r |
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Title | Transaldolase from Bacillus subtilis |
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Components | Transaldolase |
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Keywords | TRANSFERASE / transaldolase / pentose phosphate pathway / Schiff Bases |
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Function / homology | Function and homology information
transaldolase / transaldolase activity / aldehyde-lyase activity / pentose-phosphate shunt / carbohydrate metabolic process / identical protein binding / cytoplasmSimilarity search - Function Transaldolase type 3B, putative / Transaldolase type 3B/Fructose-6-phosphate aldolase / Transaldolase/Fructose-6-phosphate aldolase, archaeal/bacterial / Transaldolase active site. / Transaldolase, active site / Transaldolase signature 1. / Transaldolase/Fructose-6-phosphate aldolase / Transaldolase/Fructose-6-phosphate aldolase / Aldolase class I / Aldolase-type TIM barrel ...Transaldolase type 3B, putative / Transaldolase type 3B/Fructose-6-phosphate aldolase / Transaldolase/Fructose-6-phosphate aldolase, archaeal/bacterial / Transaldolase active site. / Transaldolase, active site / Transaldolase signature 1. / Transaldolase/Fructose-6-phosphate aldolase / Transaldolase/Fructose-6-phosphate aldolase / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Alpha BetaSimilarity search - Domain/homology |
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Biological species | ![](img/tx_bacteria.gif) Bacillus subtilis (bacteria) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å |
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Authors | Schneider, G. / Sandalova, T. / Samland, A. |
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Citation | Journal: Febs J. / Year: 2012 Title: Conservation of structure and mechanism within the transaldolase enzyme family. Authors: Samland, A.K. / Baier, S. / Schurmann, M. / Inoue, T. / Huf, S. / Schneider, G. / Sprenger, G.A. / Sandalova, T. |
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History | Deposition | Mar 24, 2011 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Feb 8, 2012 | Provider: repository / Type: Initial release |
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Revision 1.1 | Mar 21, 2012 | Group: Database references |
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Revision 1.2 | Mar 7, 2018 | Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site |
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Revision 1.3 | Jan 29, 2020 | Group: Advisory / Derived calculations Category: pdbx_distant_solvent_atoms / pdbx_struct_assembly ...pdbx_distant_solvent_atoms / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop Item: _pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details ..._pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_assembly_prop.value |
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Revision 1.4 | Sep 13, 2023 | 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 / struct_ncs_dom_lim / struct_site 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 / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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