Magnesium in PDB 1elx: E. Coli Alkaline Phosphatase Mutant (S102A)

All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant (S102A):
3.1.3.1;

The structure of E. Coli Alkaline Phosphatase Mutant (S102A), PDB code: 1elx was solved by B.Stec, M.Hehir, C.Brennan, M.Nolte, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	9.00 / 2.60
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	163.620, 163.620, 138.880, 90.00, 90.00, 120.00
R / Rfree (%)	15.8 / 20.7

The structure of E. Coli Alkaline Phosphatase Mutant (S102A) also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Magnesium atom in the E. Coli Alkaline Phosphatase Mutant (S102A) (pdb code 1elx). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the E. Coli Alkaline Phosphatase Mutant (S102A), PDB code: 1elx:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E. Coli Alkaline Phosphatase Mutant (S102A)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of E. Coli Alkaline Phosphatase Mutant (S102A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:2.0 occ:0.89 OE2 A:GLU322 1.8 10.4 1.0 O A:HOH455 1.9 2.0 1.0 OD2 A:ASP51 2.1 2.0 1.0 O A:HOH454 2.1 5.2 1.0 OG1 A:THR155 2.5 2.0 1.0 O A:HOH456 2.8 2.0 1.0 CB A:THR155 2.9 3.2 1.0 CD A:GLU322 3.0 21.0 1.0 CG A:ASP51 3.3 5.4 1.0 OE1 A:GLU322 3.5 13.8 1.0 OD2 A:ASP153 3.8 4.7 1.0 N A:THR155 3.8 2.0 1.0 CA A:THR155 3.9 2.1 1.0 CG2 A:THR155 3.9 11.8 1.0 CB A:ASP51 4.1 3.0 1.0 CB A:ALA324 4.1 7.6 1.0 OD1 A:ASP51 4.2 2.0 1.0 CG A:GLU322 4.2 9.7 1.0 CD A:PRO156 4.5 2.0 1.0 CG A:ASP153 4.5 7.5 1.0 CB A:ALA102 4.6 8.5 1.0 O4 A:PO4453 4.7 2.0 1.0 CA A:ALA324 4.8 2.0 1.0 O A:HOH654 4.9 13.1 1.0

Magnesium binding site 2 out of 2 in the E. Coli Alkaline Phosphatase Mutant (S102A)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of E. Coli Alkaline Phosphatase Mutant (S102A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg452 b:2.0 occ:1.00 O B:HOH455 1.8 2.0 1.0 O B:HOH454 1.9 9.8 1.0 OE2 B:GLU322 2.0 2.0 1.0 OD2 B:ASP51 2.2 3.9 1.0 O B:HOH456 2.4 2.0 1.0 OG1 B:THR155 2.4 10.2 1.0 CD B:GLU322 3.0 10.7 1.0 CB B:THR155 3.1 12.7 1.0 CG B:ASP51 3.3 7.3 1.0 OE1 B:GLU322 3.4 4.2 1.0 OD2 B:ASP153 3.7 2.0 1.0 N B:THR155 4.0 6.7 1.0 CB B:ASP51 4.1 9.6 1.0 CB B:ALA324 4.1 2.5 1.0 CA B:THR155 4.1 7.1 1.0 CG2 B:THR155 4.2 14.8 1.0 OD1 B:ASP51 4.2 13.5 1.0 CG B:GLU322 4.3 13.6 1.0 CD B:PRO156 4.5 2.0 1.0 O4 B:PO4453 4.5 2.0 1.0 CG B:ASP153 4.5 10.7 1.0 CA B:ALA324 4.6 2.3 1.0 O B:HOH625 4.7 34.6 1.0 CB B:ALA102 4.7 6.1 1.0 CB B:ALA149 5.0 2.0 1.0

B.Stec, M.J.Hehir, C.Brennan, M.Nolte, E.R.Kantrowitz. Kinetic and X-Ray Structural Studies of Three Mutant E. Coli Alkaline Phosphatases: Insights Into the Catalytic Mechanism Without the Nucleophile SER102. J.Mol.Biol. V. 277 647 1998.
ISSN: ISSN 0022-2836
PubMed: 9533886
DOI: 10.1006/JMBI.1998.1635