Entry | Database: PDB / ID: 4hnk |
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Title | Crystal structure of an Enzyme |
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Components | ATP-dependent Clp protease proteolytic subunit |
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Keywords | HYDROLASE / Structural Genomics Consortium / SGC / alpha/beta fold / Protease |
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Function / homology | Function and homology information
apicoplast / endopeptidase Clp complex / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / ATPase binding / serine-type endopeptidase activity / proteolysisSimilarity search - Function ATP-dependent Clp protease proteolytic subunit / Clp protease proteolytic subunit /Translocation-enhancing protein TepA / Clp protease / 2-enoyl-CoA Hydratase; Chain A, domain 1 / 2-enoyl-CoA Hydratase; Chain A, domain 1 / ClpP/crotonase-like domain superfamily / Alpha-Beta Complex / Alpha BetaSimilarity search - Domain/homology |
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Biological species | ![](img/tx_eukaryote.gif) Plasmodium falciparum (malaria parasite P. falciparum) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.9 Å |
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Authors | El Bakkouri, M. / Calmettes, C. / Wernimont, A.K. / Houry, W.A. / Hui, R. / Structural Genomics Consortium (SGC) |
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Citation | Journal: J.Biol.Chem. / Year: 2013 Title: Structural Insights into the Inactive Subunit of the Apicoplast-localized Caseinolytic Protease Complex of Plasmodium falciparum. Authors: El Bakkouri, M. / Rathore, S. / Calmettes, C. / Wernimont, A.K. / Liu, K. / Sinha, D. / Asad, M. / Jung, P. / Hui, R. / Mohmmed, A. / Houry, W.A. |
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History | Deposition | Oct 19, 2012 | Deposition site: RCSB / Processing site: RCSB |
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Revision 1.0 | Dec 5, 2012 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jan 2, 2013 | Group: Database references |
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Revision 1.2 | Jan 30, 2013 | Group: Database references |
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Revision 1.3 | Feb 28, 2024 | Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id |
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