Magnesium in PDB 3cmr: E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate

All present enzymatic activity of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate:
3.1.3.1;

The structure of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate, PDB code: 3cmr was solved by P.J.O'brien, J.K.Lassila, T.D.Fenn, J.G.Zalatan, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.75 / 2.05
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	160.614, 160.614, 139.923, 90.00, 90.00, 120.00
R / Rfree (%)	18 / 21.3

The structure of E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Magnesium atom in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate (pdb code 3cmr). 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 R166S in Complex with Phosphate, PDB code: 3cmr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate


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 R166S in Complex with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg453 b:29.7 occ:1.00 O A:HOH501 2.2 26.6 1.0 O A:HOH503 2.2 30.6 1.0 OD2 A:ASP51 2.2 32.4 1.0 OE2 A:GLU322 2.2 35.8 1.0 O A:HOH502 2.2 29.3 1.0 OG1 A:THR155 2.3 30.9 1.0 CG A:ASP51 3.2 33.2 1.0 CD A:GLU322 3.2 36.6 1.0 CB A:THR155 3.3 33.8 1.0 OE1 A:GLU322 3.6 29.1 1.0 OD2 A:ASP153 3.7 33.2 1.0 CB A:ASP51 3.8 33.1 1.0 O A:HOH557 4.1 28.1 1.0 N A:THR155 4.1 32.3 1.0 OD1 A:ASP51 4.2 31.7 1.0 CB A:SER102 4.2 33.4 1.0 CA A:THR155 4.3 33.2 1.0 O A:HOH506 4.3 24.2 1.0 OG A:SER102 4.3 34.2 1.0 CG2 A:THR155 4.4 34.4 1.0 CB A:ALA324 4.4 32.9 1.0 CG A:GLU322 4.5 36.4 1.0 CG A:ASP153 4.6 34.4 1.0 O2 A:PO4452 4.6 43.6 1.0 ZN A:ZN450 4.6 28.7 1.0 CA A:ALA324 4.7 33.6 1.0 O A:ALA324 4.8 33.1 1.0 OD2 A:ASP369 4.8 33.9 1.0

Magnesium binding site 2 out of 2 in the E. Coli Alkaline Phosphatase Mutant R166S in Complex with Phosphate


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 R166S in Complex with Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg453 b:34.7 occ:1.00 OE2 B:GLU322 2.1 35.3 1.0 O B:HOH503 2.1 33.0 1.0 O B:HOH501 2.2 32.9 1.0 O B:HOH502 2.2 34.5 1.0 OD2 B:ASP51 2.2 30.0 1.0 OG1 B:THR155 2.3 33.1 1.0 CD B:GLU322 3.1 35.9 1.0 CG B:ASP51 3.2 33.8 1.0 CB B:THR155 3.3 33.1 1.0 OE1 B:GLU322 3.4 32.1 1.0 CB B:ASP51 3.8 34.1 1.0 OD2 B:ASP153 3.9 36.7 1.0 N B:THR155 4.1 33.0 1.0 OD1 B:ASP51 4.2 32.9 1.0 O B:HOH525 4.3 27.1 1.0 CA B:THR155 4.3 33.0 1.0 CG2 B:THR155 4.3 33.2 1.0 O B:HOH509 4.3 26.5 1.0 CB B:SER102 4.3 31.9 1.0 OG B:SER102 4.3 33.8 1.0 CB B:ALA324 4.4 32.6 1.0 CG B:GLU322 4.4 36.1 1.0 CG B:ASP153 4.7 34.2 1.0 ZN B:ZN450 4.7 33.1 1.0 CA B:ALA324 4.7 32.2 1.0 OD2 B:ASP369 4.8 32.6 1.0 O2 B:PO4452 4.8 43.3 1.0 O B:ALA324 4.8 31.4 1.0

P.J.O'brien, J.K.Lassila, T.D.Fenn, J.G.Zalatan, D.Herschlag. Arginine Coordination in Enzymatic Phosphoryl Transfer: Evaluation of the Effect of ARG166 Mutations in Escherichia Coli Alkaline Phosphatase Biochemistry V. 47 7663 2008.
ISSN: ISSN 0006-2960
PubMed: 18627128
DOI: 10.1021/BI800545N