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TitleStructural Analysis of the L-Alanoyl-D-Glutamate Endopeptidase Domain of Listeria Bacteriophage Endolysin Ply500 Reveals a New Member of the Las Peptidase Family.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 64, Page 644-, Year 2008
Publish dateFeb 9, 2008 (structure data deposition date)
AuthorsKorndorfer, I.P. / Kanitz, A. / Danzer, J. / Zimmer, M. / Loessner, M.J. / Skerra, A.
External linksActa Crystallogr. ,Sect. D / PubMed:18560152
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-2vo9:
CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • bacteriophage a500 (virus)
KeywordsHYDROLASE / CELL WALL BIOGENESIS/DEGRADATION / SECRETED / CELL WALL

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