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TitleMutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
Journal, issue, pagesJ. Mol. Biol., Vol. 253, Page 604-617, Year 1995
Publish dateSep 6, 1995 (structure data deposition date)
AuthorsMurphy, J.E. / Tibbitts, T.T. / Kantrowitz, E.R.
External linksJ. Mol. Biol. / PubMed:7473737
MethodsX-ray diffraction
Resolution2.3 - 2.5 Å
Structure data

PDB-1ani:
ALKALINE PHOSPHATASE (D153H, K328H)
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1anj:
ALKALINE PHOSPHATASE (K328H)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-2anh:
ALKALINE PHOSPHATASE (D153H)
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsALKALINE PHOSPHATASE / HYDROLASE (PHOSPHORIC MONOESTER) / TRANSFERASE (PHOSPHO / ALCOHOL ACCEPTOR)

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