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TitleHydrophobic surface residues can stabilize a protein through improved water-protein interactions.
Journal, issue, pagesFebs J., Year 2019
Publish dateJul 1, 2017 (structure data deposition date)
AuthorsIslam, M.M. / Kobayashi, K. / Kidokoro, S.I. / Kuroda, Y.
External linksFebs J. / PubMed:31175706
MethodsX-ray diffraction
Resolution1.12 - 1.67 Å
Structure data

PDB-5xx2:
A BPTI-[5,55] variant with C14GA38L mutations
Method: X-RAY DIFFRACTION / Resolution: 1.12 Å

PDB-5xx3:
A BPTI-[5,55] variant with C14GA38G mutations
Method: X-RAY DIFFRACTION / Resolution: 1.12 Å

PDB-5xx4:
A BPTI-[5,55] variant with C14GA38K mutations
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-5xx5:
A BPTI-[5,55] variant with C14GA38I mutations
Method: X-RAY DIFFRACTION / Resolution: 1.38 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • bos taurus (domestic cattle)
KeywordsHYDROLASE / HYDROLASE INHIBITOR

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