登録情報 | データベース: PDB / ID: 2fq6 |
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タイトル | Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide |
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要素 | Cystathionine beta-lyase |
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キーワード | LYASE (リアーゼ) / PROTEIN-INHIBITOR COMPLEX / PLP COFACTOR COVALENTLY BOUND TO P3F INHIBITOR |
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機能・相同性 | 機能・相同性情報
L-cysteine desulfidase / L-cysteine catabolic process to pyruvate / cysteine-S-conjugate beta-lyase activity / cysteine-S-conjugate beta-lyase / : / alanine racemase activity / L-cysteine desulfhydrase activity / methionine biosynthetic process / transsulfuration / pyridoxal phosphate binding ...L-cysteine desulfidase / L-cysteine catabolic process to pyruvate / cysteine-S-conjugate beta-lyase activity / cysteine-S-conjugate beta-lyase / : / alanine racemase activity / L-cysteine desulfhydrase activity / methionine biosynthetic process / transsulfuration / pyridoxal phosphate binding / protein homotetramerization / protein-containing complex / identical protein binding / 細胞質類似検索 - 分子機能 Cystathionine beta-lyase, bacterial / Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. / Cys/Met metabolism, pyridoxal phosphate-dependent enzyme / Cys/Met metabolism PLP-dependent enzyme / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain ...Cystathionine beta-lyase, bacterial / Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. / Cys/Met metabolism, pyridoxal phosphate-dependent enzyme / Cys/Met metabolism PLP-dependent enzyme / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Alpha Beta類似検索 - ドメイン・相同性 |
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生物種 | Escherichia coli (大腸菌) |
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手法 | X線回折 / 分子置換 / 解像度: 1.78 Å |
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データ登録者 | Junop, M.S. |
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引用 | ジャーナル: J.Med.Chem. / 年: 2007 タイトル: Inhibitors of bacterial cystathionine beta-lyase: leads for new antimicrobial agents and probes of enzyme structure and function. 著者: Ejim, L.J. / Blanchard, J.E. / Koteva, K.P. / Sumerfield, R. / Elowe, N.H. / Chechetto, J.D. / Brown, E.D. / Junop, M.S. / Wright, G.D. |
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履歴 | 登録 | 2006年1月17日 | 登録サイト: RCSB / 処理サイト: RCSB |
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改定 1.0 | 2006年12月26日 | Provider: repository / タイプ: Initial release |
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改定 1.1 | 2008年5月1日 | Group: Version format compliance |
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改定 1.2 | 2011年7月13日 | Group: Derived calculations / Version format compliance |
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改定 1.3 | 2023年8月30日 | Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description カテゴリ: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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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