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TitleAsp79 Makes a Large, Unfavorable Contribution to the Stability of RNase Sa.
Journal, issue, pagesJ. Mol. Biol., Vol. 354, Page 967-978, Year 2005
Publish dateJan 25, 2005 (structure data deposition date)
AuthorsTrevino, S.R. / Gokulan, K. / Newsom, S. / Thurlkill, R.L. / Shaw, K.L. / Mitkevich, V.A. / Makarov, A.A. / Sacchettini, J.C. / Scholtz, J.M. / Pace, C.N.
External linksJ. Mol. Biol. / PubMed:16288913
MethodsX-ray diffraction
Resolution1.2 Å
Structure data

PDB-1ynv:
Asp79 makes a large, unfavorable contribution to the stability of RNase Sa
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • streptomyces aureofaciens (bacteria)
KeywordsHYDROLASE / Conformational stability / electrostatic strain / pKa / hydrogen bonds and ion pair.

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