Magnesium in PDB 1alj: Alkaline Phosphatase Mutant (H412N)

All present enzymatic activity of Alkaline Phosphatase Mutant (H412N):
3.1.3.1;

The structure of Alkaline Phosphatase Mutant (H412N), PDB code: 1alj was solved by L.Ma, T.T.Tibbitts, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.60
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	194.760, 167.740, 76.230, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / n/a

The structure of Alkaline Phosphatase Mutant (H412N) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Alkaline Phosphatase Mutant (H412N) (pdb code 1alj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Alkaline Phosphatase Mutant (H412N), PDB code: 1alj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:51.6 occ:1.00 O A:HOH500 2.5 69.8 1.0 OG1 A:THR155 2.7 14.2 1.0 OE2 A:GLU322 2.7 11.2 1.0 OD1 A:ASP51 2.7 91.6 1.0 O A:HOH454 2.9 50.1 0.7 OD2 A:ASP51 3.1 95.3 1.0 CG A:ASP51 3.1 80.9 1.0 O A:HOH456 3.3 75.5 0.8 OD2 A:ASP153 3.5 26.3 1.0 CB A:THR155 3.6 4.0 1.0 CD A:GLU322 3.8 2.0 1.0 N A:THR155 3.9 5.0 1.0 CB A:SER102 4.0 10.2 1.0 OG A:SER102 4.0 29.1 1.0 OE1 A:GLU322 4.2 9.1 1.0 O A:HOH524 4.2 36.8 1.0 OD2 A:ASP369 4.3 36.0 1.0 CA A:THR155 4.4 11.5 1.0 CG A:ASP153 4.4 14.9 1.0 CB A:ASP51 4.4 47.8 1.0 ZN A:ZN451 4.5 45.9 0.2 CG2 A:THR155 4.8 2.6 1.0

Magnesium binding site 2 out of 2 in the Alkaline Phosphatase Mutant (H412N)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Alkaline Phosphatase Mutant (H412N) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg452 b:48.9 occ:0.96 OG1 B:THR155 2.5 19.1 1.0 O B:HOH519 3.0 52.4 0.8 OE2 B:GLU322 3.0 25.5 1.0 OD1 B:ASP51 3.1 81.5 1.0 O B:HOH520 3.3 74.9 0.6 OD2 B:ASP153 3.3 34.7 1.0 CB B:THR155 3.4 13.4 1.0 N B:THR155 3.4 11.0 1.0 CG B:ASP51 3.6 71.5 1.0 OD2 B:ASP51 3.7 84.0 1.0 CB B:SER102 3.8 4.5 1.0 CD B:GLU322 4.0 7.8 1.0 CA B:THR155 4.0 15.5 1.0 O B:HOH548 4.0 23.7 1.0 OG B:SER102 4.0 30.0 1.0 CG B:ASP153 4.2 23.7 1.0 OE1 B:GLU322 4.2 12.1 1.0 OD2 B:ASP369 4.4 27.8 1.0 C B:ALA154 4.4 12.9 1.0 CB B:ALA154 4.4 4.4 1.0 N B:ALA154 4.6 11.4 1.0 ZN B:ZN451 4.6 54.6 0.4 CA B:ALA154 4.6 12.6 1.0 CG2 B:THR155 4.6 14.4 1.0 OD1 B:ASP153 4.8 21.3 1.0 CD B:PRO156 4.8 9.0 1.0 CB B:ASP51 4.9 42.0 1.0 CB B:ASP153 5.0 15.3 1.0

L.Ma, T.T.Tibbitts, E.R.Kantrowitz. Escherichia Coli Alkaline Phosphatase: X-Ray Structural Studies of A Mutant Enzyme (His-412-->Asn) at One of the Catalytically Important Zinc Binding Sites. Protein Sci. V. 4 1498 1995.
ISSN: ISSN 0961-8368
PubMed: 8520475