CRYSTAL STRUCTURE OF THE HYBRID C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FORMED BY HYBRIDIZING THE SCAFFOLD OF THE ESCHERICHIA COLI ENZYME WITH THE ACTIVE SITE LOOPS FROM THE THERMOANAEROBACTER TENGCONGENSIS ENZYME
收藏Protein Data Bank Japan2023-10-11 更新2026-03-21 收录
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https://pdbj.org/mine/summary/6v9k
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CRYSTAL STRUCTURE OF THE HYBRID C-TERMINAL DOMAIN OF ENZYME I OF THE BACTERIAL PHOSPHOTRANSFERASE SYSTEM FORMED BY HYBRIDIZING THE SCAFFOLD OF THE ESCHERICHIA COLI ENZYME WITH THE ACTIVE SITE LOOPS FROM THE THERMOANAEROBACTER TENGCONGENSIS ENZYME Descriptor: MAGNESIUM ION, Phosphoenolpyruvate-protein phosphotransferase Authors: Stewart Jr, C.E. Deposit date: 2019-12-13 Release date: 2020-06-17 Last modified: 2023-10-11 Method: X-RAY DIFFRACTION (1.9 Å) Cite: Hybrid Thermophilic/Mesophilic Enzymes Reveal a Role for Conformational Disorder in Regulation of Bacterial Enzyme I. J.Mol.Biol., 432, 2020
创建时间：
2019-12-13
