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Structure paper

TitleCoordination Sphere of the Third Metal Site is Essential to the Activity and Metal Selectivity of Alkaline Phosphatases.
Journal, issue, pagesProtein Sci., Vol. 19, Page 75-, Year 2010
Publish dateDec 15, 2008 (structure data deposition date)
AuthorsKoutsioulis, D. / Lyskowski, A. / Maki, S. / Guthrie, E. / Feller, G. / Bouriotis, V. / Heikinheimo, P.
External linksProtein Sci. / PubMed:19916164
MethodsX-ray diffraction
Resolution1.78 - 1.99 Å
Structure data

PDB-2w5v:
Structure of TAB5 alkaline phosphatase mutant His 135 Asp with Mg bound in the M3 site.
Method: X-RAY DIFFRACTION / Resolution: 1.78 Å

PDB-2w5w:
Structure of TAB5 alkaline phosphatase mutant His 135 Asp with Zn bound in the M3 site.
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

PDB-2w5x:
Structure of TAB5 alkaline phosphatase mutant His 135 Glu with Mg bound in the M3 site.
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • antarctic bacterium tab5 (bacteria)
KeywordsHYDROLASE / PSYCHROPHILES / COLD ADAPTATION / ALKALINE PHOSPHATASE

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