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TitleStructural Analysis of Papain-Like NlpC/P60 Superfamily Enzymes with a Circularly Permuted Topology Reveals Potential Lipid Binding Sites.
Journal, issue, pagesPlos One, Vol. 6, Page e22013-e22013, Year 2011
Publish dateNov 30, 2009 (structure data deposition date)
AuthorsXu, Q. / Rawlings, N.D. / Chiu, H.J. / Jaroszewski, L. / Klock, H.E. / Knuth, M.W. / Miller, M.D. / Elsliger, M.A. / Deacon, A.M. / Godzik, A. ...Xu, Q. / Rawlings, N.D. / Chiu, H.J. / Jaroszewski, L. / Klock, H.E. / Knuth, M.W. / Miller, M.D. / Elsliger, M.A. / Deacon, A.M. / Godzik, A. / Lesley, S.A. / Wilson, I.A.
External linksPlos One / PubMed:21799766
MethodsX-ray diffraction
Resolution2.5 Å
Structure data

PDB-3kw0:
Crystal structure of Cysteine peptidase (NP_982244.1) from BACILLUS CEREUS ATCC 10987 at 2.50 A resolution
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-LYS:
LYSINE

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • bacillus cereus (bacteria)
KeywordsHYDROLASE / Cysteine peptidase / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2

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