4XCM

Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus

Summary for 4XCM

• Entry DOI: 10.2210/pdb4xcm/pdb
• Descriptor: Cell wall-binding endopeptidase-related protein (2 entities in total)
• Functional Keywords: nlpc/p60, d, l-endopeptidase, lysm domain, hydrolase
• Biological source: Thermus thermophilus HB8
• Total number of polymer chains: 2
• Total formula weight: 53379.93

Authors

Wong, J.,Midtgaard, S.,Gysel, K.,Thygesen, M.B.,Sorensen, K.K.,Jensen, K.J.,Stougaard, J.,Thirup, S.,Blaise, M. (deposition date: 2014-12-18, release date: 2015-01-14, Last modification date: 2018-01-17)

• Primary citation: Wong, J.E.,Midtgaard, S.R.,Gysel, K.,Thygesen, M.B.,Srensen, K.K.,Jensen, K.J.,Stougaard, J.,Thirup, S.,Blaise, M.; An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase.; Acta Crystallogr.,Sect.D, 71:592-605, 2015; PubMed: 25760608; DOI: 10.1107/S139900471402793X

Experimental method

X-RAY DIFFRACTION (2.65 Å)