ALKALINE PHOSPHATASE (E.C. 3.1.3.1) COMPLEX WITH MERCAPTOMETHYL PHOSPHONATE

Alternate modes of binding in two crystal structures of alkaline phosphatase-inhibitor complexes.

A Model of the Transition State in the Alkaline Phosphatase Reaction

Reaction Mechanism of Alkaline Phosphatase Based on Two Crystal Structures. Two-metal Ion Catalysis

enzyme: 30 mg/mL; buffer: 40% saturated ammonium sulfate, 100 mM Tris/10 mM magnesium sulfate, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 25K

E.coli Alkaline Phosphatase Complex With Vanadate

E.coli Alkaline Phosphatase Complex With Phosphonoacetic Acid

Myers, JK, Antonelli, SM, Widlanski, TS. 1997. Motifs for metallophosphatase inhibition. J. Am. Chem. Soc. 119: 3163-3164.

The magnesium 452 has three waters associated with it and
it has been labelled as ligand MO3 for each chain.
The zinc ion 452 has the same three waters associated with
it and is labelled ZO3. The ZO3 and MO3 occupy the same
space and have the same coordinates, but their occupancies
are different. The MO3 is labelled as residue 452,
conformation A. The ZO3 is labelled as residue 453,
conformation B.
SO4 558 is ASSOCIATED WITH CHAIN A, and SO4 958 is
ASSOCIATED WITH CHAIN B.

Used conjugated gradient least
squares for the refinement and
weighted full matrix least squares
procedure for estimating ESDs.

homodimeric metalloenzyme with a non-crystallographic 2-fold symmetry axis