Magnesium in PDB 3bdh: Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase

All present enzymatic activity of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase:
3.1.3.1;

The structure of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase, PDB code: 3bdh was solved by J.C.Grigg, M.E.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	55.449, 103.545, 88.489, 90.00, 105.76, 90.00
R / Rfree (%)	15.2 / 18.9

The binding sites of Magnesium atom in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase (pdb code 3bdh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase, PDB code: 3bdh:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:14.6 occ:1.00 O A:HOH1059 2.1 9.8 1.0 O A:HOH1032 2.1 16.0 1.0 OE2 A:GLU322 2.1 9.8 1.0 OG1 A:THR155 2.1 8.7 1.0 O A:HOH1056 2.2 11.5 1.0 O A:HOH520 2.2 14.4 1.0 CD A:GLU322 3.1 10.4 1.0 CB A:THR155 3.1 7.3 1.0 OE1 A:GLU322 3.4 9.4 1.0 OD2 A:ASP153 3.7 13.1 1.0 N A:THR155 4.0 7.8 1.0 OD2 A:ASP51 4.1 17.3 1.0 CG2 A:THR155 4.2 8.2 1.0 CA A:THR155 4.2 8.1 1.0 O A:HOH502 4.2 10.0 1.0 CB A:SER102 4.4 9.7 1.0 OD2 A:ASP369 4.4 12.2 1.0 OG A:SER102 4.4 18.2 1.0 CG A:GLU322 4.4 9.1 1.0 CG A:ASP51 4.5 14.8 1.0 O A:HOH1012 4.5 38.2 1.0 CB A:ASP51 4.6 11.8 1.0 CG A:ASP153 4.6 11.5 1.0 O A:HOH1014 4.7 20.0 1.0 CB A:ALA324 4.8 14.9 1.0 CD A:PRO156 4.9 9.1 1.0 O A:HOH1057 5.0 22.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Zinc-Deficient Wild-Type E. Coli Alkaline Phosphatase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg500 b:13.5 occ:1.00 O B:HOH1070 2.1 11.7 1.0 O B:HOH1065 2.1 12.1 1.0 OE2 B:GLU322 2.1 10.0 1.0 O B:HOH1056 2.1 10.1 1.0 O B:HOH508 2.1 8.5 1.0 OG1 B:THR155 2.2 9.5 1.0 CD B:GLU322 3.1 10.4 1.0 CB B:THR155 3.2 7.6 1.0 OE1 B:GLU322 3.5 10.2 1.0 OD2 B:ASP153 3.6 13.9 1.0 N B:THR155 4.0 8.2 1.0 OD2 B:ASP51 4.1 17.5 1.0 O B:HOH505 4.2 8.4 1.0 CA B:THR155 4.2 8.3 1.0 CG2 B:THR155 4.2 8.7 1.0 OD2 B:ASP369 4.3 11.7 1.0 OG B:SER102 4.4 19.1 1.0 CG B:GLU322 4.4 10.2 1.0 CB B:SER102 4.4 9.6 1.0 CG B:ASP51 4.4 13.8 1.0 CB B:ASP51 4.6 10.6 1.0 CG B:ASP153 4.6 12.8 1.0 O B:HOH1032 4.6 22.2 1.0 CB B:ALA324 4.7 11.0 1.0 CD B:PRO156 5.0 8.4 1.0

J.C.Grigg, C.Hucaluk, M.E.Murphy, H.Ritter, J.Yee, S.Rafferty. The Active-Site Trimetallic Cluster of Alkaline Phosphatase Is Lost Upon Isosteric Mutation at the MG2+-Coordinating Residue Threonine-155 To Be Published.