Entry | Database: PDB / ID: 8j9f |
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Title | Structure of STG-hydrolyzing beta-glucosidase 1 (PSTG1) |
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Components | Beta-glucosidase |
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Keywords | HYDROLASE / GH3 family / sesaminol biosynthesis |
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Function / homology | Function and homology information
scopolin beta-glucosidase activity / beta-glucosidase / beta-glucosidase activity / carbohydrate metabolic processSimilarity search - Function Fibronectin type III-like domain / Fibronectin type III-like domain / Fibronectin type III-like domain / Glycoside hydrolase, family 3, active site / Glycosyl hydrolases family 3 active site. / Glycoside hydrolase family 3 C-terminal domain / Glycosyl hydrolase family 3 C-terminal domain / Glycoside hydrolase family 3 C-terminal domain superfamily / Glycoside hydrolase, family 3, N-terminal / Glycoside hydrolase, family 3, N-terminal domain superfamily ...Fibronectin type III-like domain / Fibronectin type III-like domain / Fibronectin type III-like domain / Glycoside hydrolase, family 3, active site / Glycosyl hydrolases family 3 active site. / Glycoside hydrolase family 3 C-terminal domain / Glycosyl hydrolase family 3 C-terminal domain / Glycoside hydrolase family 3 C-terminal domain superfamily / Glycoside hydrolase, family 3, N-terminal / Glycoside hydrolase, family 3, N-terminal domain superfamily / Glycosyl hydrolase family 3 N terminal domain / Glycoside hydrolase superfamily / Immunoglobulin-like foldSimilarity search - Domain/homology |
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Biological species | Paenibacillus relictisesami (bacteria) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.85 Å |
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Authors | Yanai, T. / Imaizumi, R. / Takahashi, Y. / Katsumura, E. / Yamamoto, M. / Nakayama, T. / Yamashita, S. / Takeshita, K. / Sakai, N. / Matsuura, H. |
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Funding support | Japan, 2items Organization | Grant number | Country |
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Japan Society for the Promotion of Science (JSPS) | 23H05470 | Japan | Japan Agency for Medical Research and Development (AMED) | | Japan |
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Citation | Journal: J.Biochem. / Year: 2023 Title: Structural insights into a bacterial beta-glucosidase capable of degrading sesaminol triglucoside to produce sesaminol: toward the understanding of the aglycone recognition mechanism by the C-terminal lid domain. Authors: Yanai, T. / Takahashi, Y. / Katsumura, E. / Sakai, N. / Takeshita, K. / Imaizumi, R. / Matsuura, H. / Hongo, S. / Waki, T. / Takahashi, S. / Yamamoto, M. / Kataoka, K. / Nakayama, T. / Yamashita, S. |
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History | Deposition | May 3, 2023 | Deposition site: PDBJ / Processing site: PDBJ |
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Revision 1.0 | Apr 10, 2024 | Provider: repository / Type: Initial release |
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Revision 1.1 | Jul 17, 2024 | Group: Database references / Category: citation / citation_author 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 |
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