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Structure paper

TitleKinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase.
Journal, issue, pagesJ. Mol. Biol., Vol. 257, Page 700-715, Year 1996
Publish dateFeb 3, 1996 (structure data deposition date)
AuthorsTibbitts, T.T. / Murphy, J.E. / Kantrowitz, E.R.
External linksJ. Mol. Biol. / PubMed:8648634
MethodsX-ray diffraction
Resolution2.04 - 2.14 Å
Structure data

PDB-1ura:
ALKALINE PHOSPHATASE (D51ZN)
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

PDB-1urb:
ALKALINE PHOSPHATASE (N51MG)
Method: X-RAY DIFFRACTION / Resolution: 2.14 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

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

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