+Search query
-Structure paper
Title | Mutations 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, pages | J. Mol. Biol., Vol. 253, Page 604-617, Year 1995 |
Publish date | Sep 6, 1995 (structure data deposition date) |
Authors | Murphy, J.E. / Tibbitts, T.T. / Kantrowitz, E.R. |
External links | J. Mol. Biol. / PubMed:7473737 |
Methods | X-ray diffraction |
Resolution | 2.3 - 2.5 Å |
Structure data | PDB-1ani: PDB-1anj: PDB-2anh: |
Chemicals | ChemComp-ZN: ChemComp-PO4: ChemComp-HOH: |
Source |
|
Keywords | ALKALINE PHOSPHATASE / HYDROLASE (PHOSPHORIC MONOESTER) / TRANSFERASE (PHOSPHO / ALCOHOL ACCEPTOR) |