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5A6S

Crystal structure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product

Summary for 5A6S
Entry DOI10.2210/pdb5a6s/pdb
DescriptorENDOLYSIN, SULFATE ION, GLYCEROL, ... (6 entities in total)
Functional Keywordsstructural protein, endolysin, secondary translation product, bacteriophage
Biological sourceCLOSTRIDIUM PHAGE PHICTP1
More
Total number of polymer chains2
Total formula weight42518.92
Authors
Dunne, M.,Leicht, S.,Krichel, B.,Mertens, H.D.T.,Thompson, A.,Krijgsveld, J.,Svergun, D.I.,GomezTorres, N.,Garde, S.,Uetrecht, C.,Narbad, A.,Mayer, M.J.,Meijers, R. (deposition date: 2015-07-01, release date: 2015-12-30, Last modification date: 2024-01-10)
Primary citationDunne, M.,Leicht, S.,Krichel, B.,Mertens, H.D.T.,Thompson, A.,Krijgsveld, J.,Svergun, D.I.,Gomez-Torres, N.,Garde, S.,Uetrecht, C.,Narbad, A.,Mayer, M.J.,Meijers, R.
Crystal Structure of the Ctp1L Endolysin Reveals How its Activity is Regulated by a Secondary Translation Product.
J.Biol.Chem., 291:4882-, 2016
Cited by
PubMed: 26683375
DOI: 10.1074/JBC.M115.671172
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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