2VO9

CRYSTAL STRUCTURE OF THE ENZYMATICALLY ACTIVE DOMAIN OF THE LISTERIA MONOCYTOGENES BACTERIOPHAGE 500 ENDOLYSIN PLY500

Replaces:  1XP2

Summary for 2VO9

• Entry DOI: 10.2210/pdb2vo9/pdb
• Descriptor: L-ALANYL-D-GLUTAMATE PEPTIDASE, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: cell wall biogenesis/degradation, secreted, cell wall, hydrolase
• Biological source: BACTERIOPHAGE A500
• Total number of polymer chains: 3
• Total formula weight: 60149.53

Authors

Korndoerfer, I.P.,Kanitz, A.,Skerra, A. (deposition date: 2008-02-09, release date: 2008-02-19, Last modification date: 2024-05-08)

• Primary citation: Korndorfer, I.P.,Kanitz, A.,Danzer, J.,Zimmer, M.,Loessner, M.J.,Skerra, A.; 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, 64:644-, 2008; PubMed: 18560152; DOI: 10.1107/S0907444908007890

Experimental method

X-RAY DIFFRACTION (1.8 Å)