CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500
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https://pdbj.org/mine/summary/2vo9
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CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500 Descriptor: L-ALANYL-D-GLUTAMATE PEPTIDASE, SULFATE ION, ZINC ION Authors: Korndoerfer, I.P, Kanitz, A, Skerra, A. Deposit date: 2008-02-09 Release date: 2008-02-19 Last modified: 2024-05-08 Method: X-RAY DIFFRACTION (1.8 Å) Cite: Structural Analysis of the L-Alanoyl-D-Glutamate Endopeptidase Domain of Listeria Bacteriophage Endolysin Ply500 Reveals a New Member of the Las Peptidase Family. Acta Crystallogr.,Sect.D, 64, 2008
创建时间:
2008-02-09



