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Structure paper

TitleBalancing Specificity and Promiscuity in Enzyme Evolution: Multidimensional Activity Transitions in the Alkaline Phosphatase Superfamily.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 141, Page 370-387, Year 2019
Publish dateJun 17, 2014 (structure data deposition date)
Authorsvan Loo, B. / Bayer, C.D. / Fischer, G. / Jonas, S. / Valkov, E. / Mohamed, M.F. / Vorobieva, A. / Dutruel, C. / Hyvonen, M. / Hollfelder, F.
External linksJ. Am. Chem. Soc. / PubMed:30497259
MethodsX-ray diffraction
Resolution1.25 - 2.5 Å
Structure data

PDB-4uph:
Crystal Structure of Phosphonate Monoester Hydrolase of Agrobacterium radiobacter
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-4upi:
Dimeric sulfatase SpAS1 from Silicibacter pomeroyi
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-4upk:
Phosphonate monoester hydrolase SpPMH from Silicibacter pomeroyi
Method: X-RAY DIFFRACTION / Resolution: 2.24 Å

PDB-4upl:
Dimeric sulfatase SpAS2 from Silicibacter pomeroyi
Method: X-RAY DIFFRACTION / Resolution: 1.805 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

Source
  • agrobacterium radiobacter k84 (bacteria)
  • ruegeria pomeroyi (bacteria)
KeywordsHYDROLASE / SUPERFAMILY / ALKALINE PHOSPHATASE SUPERFAMILY / ALAKALINE PHOSPHATASE SUPERFAMILY / PROMISCUITY

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