Entry | Database: PDB / ID: 3wo8 |
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Title | Crystal structure of the beta-N-acetylglucosaminidase from Thermotoga maritima |
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Components | Beta-N-acetylglucosaminidase |
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Keywords | HYDROLASE / TIM barrel / Glycosidase |
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Function / homology | Function and homology information
beta-N-acetylhexosaminidase activity / beta-N-acetylhexosaminidase / peptidoglycan turnover / N-acetyl-beta-D-galactosaminidase activity / carbohydrate metabolic processSimilarity search - Function Glycoside hydrolase, family 3, N-terminal domain / Glycoside hydrolase, family 3, N-terminal / Glycoside hydrolase, family 3, N-terminal domain superfamily / Glycosyl hydrolase family 3 N terminal domain / Glycoside hydrolase superfamily / TIM Barrel / Alpha-Beta Barrel / Alpha BetaSimilarity search - Domain/homology |
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Biological species | ![](img/tx_bacteria.gif) Thermotoga maritima (bacteria) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.43 Å |
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Authors | Mine, S. / Kado, Y. / Watanabe, M. / Inoue, T. / Ishikawa, K. |
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Citation | Journal: Febs J. / Year: 2014 Title: The structure of hyperthermophilic beta-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site. Authors: Mine, S. / Kado, Y. / Watanabe, M. / Fukuda, Y. / Abe, Y. / Ueda, T. / Kawarabayasi, Y. / Inoue, T. / Ishikawa, K. |
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History | Deposition | Dec 20, 2013 | Deposition site: PDBJ / Processing site: PDBJ |
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Revision 1.0 | Dec 24, 2014 | Provider: repository / Type: Initial release |
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Revision 1.1 | Mar 20, 2024 | Group: Data collection / Database references Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details |
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