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EBI PDBe PDBeView

PDBe Entry: 1anj view

ALKALINE PHOSPHATASE (K328H)
Summary
Header ALKALINE PHOSPHATASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.3 Å, R-factor: 19.4%, Free R-factor: 24.9%, Spacegroup: I 2 2 2
Released 29/01/1996, deposition: 06/09/1995, last revision: 24/02/2009
Authors Murphy, J.E.search; Tibbitts, T.T.search; Kantrowitz, E.R.search
Primary citation Mutations at positions 153 and 328 in Escherichia coli alkaline phosphatase provide insight towards the structure and function of mammalian and yeast alkaline phosphatases.
J.MOL.BIOL.search vol:253, pag:604-617 (1995) [PubMed ID 7473737 ]search
Keywords HYDROLASE (PHOSPHORIC MONOESTER)search, TRANSFERASE (PHOSPHOsearch, ALCOHOL ACCEPTOR)search, ALKALINE PHOSPHATASEsearch
EC 3.1.3.1 ExPASy BRENDA search (A B)
Organism Escherichia coli 562search(A B)
UniProt Alkaline phosphatase precursor (EC 3.1.3.1) (APase) P00634search (A B)
Solvent A, B
Polymers
Id Name Type UniProt Residues Observed
A, B ALKALINE PHOSPHATASE Protein P00634 (PPB_ECOLI)search
 446 100%
Heterogens
Id Name Ligands
A, B ZINC ION ZN search
A, B PHOSPHATE ION PO4 search
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