Magnesium in PDB 1urb: Alkaline Phosphatase (N51MG)

All present enzymatic activity of Alkaline Phosphatase (N51MG):
3.1.3.1;

The structure of Alkaline Phosphatase (N51MG), PDB code: 1urb was solved by T.T.Tibbitts, J.E.Murphy, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.14
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	195.720, 168.480, 76.330, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 24.1

The structure of Alkaline Phosphatase (N51MG) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Alkaline Phosphatase (N51MG) (pdb code 1urb). 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 (N51MG), PDB code: 1urb:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Alkaline Phosphatase (N51MG)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Alkaline Phosphatase (N51MG) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg451 b:16.6 occ:0.71 CE1 A:HIS370 1.9 33.2 1.0 OD2 A:ASP369 2.2 30.7 1.0 OD1 A:ASN51 2.3 26.6 1.0 OG A:SER102 2.4 27.1 1.0 NE2 A:HIS370 2.6 32.1 1.0 ND1 A:HIS370 2.6 33.7 1.0 CG A:ASP369 2.8 26.0 1.0 OD1 A:ASP369 3.0 14.2 1.0 CG A:ASN51 3.3 29.1 1.0 CB A:SER102 3.3 15.8 1.0 CD2 A:HIS370 3.5 28.6 1.0 CG A:HIS370 3.5 19.8 1.0 ND2 A:ASN51 3.7 30.7 1.0 CA A:SER102 3.8 14.8 1.0 N A:SER102 4.1 10.4 1.0 CB A:ASP369 4.1 18.8 1.0 ZN A:ZN450 4.2 27.4 0.8 O4 A:PO4453 4.3 34.3 0.6 OD1 A:ASP327 4.3 28.1 1.0 N A:GLY52 4.3 10.0 1.0 CG A:ASP327 4.4 27.2 1.0 O2 A:PO4453 4.4 23.6 0.6 OD2 A:ASP327 4.6 34.4 1.0 O1 A:PO4453 4.6 31.8 0.6 CB A:ASN51 4.6 20.7 1.0 P A:PO4453 4.6 31.2 0.6 O A:HOH628 4.7 33.1 1.0 N A:HIS370 4.7 14.6 1.0 O A:HOH694 4.7 40.9 1.0 CB A:HIS370 4.8 20.3 1.0 CA A:ASN51 4.8 12.6 1.0 C A:ASP101 4.8 14.8 1.0 C A:ASN51 4.8 12.2 1.0 CB A:ASP327 4.9 28.9 1.0 NE2 A:HIS412 4.9 33.1 1.0 CA A:GLY52 4.9 12.3 1.0

Magnesium binding site 2 out of 2 in the Alkaline Phosphatase (N51MG)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Alkaline Phosphatase (N51MG) within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg451 b:20.1 occ:0.59 OD1 B:ASN51 2.2 26.3 1.0 OG B:SER102 2.2 29.9 1.0 CE1 B:HIS370 2.3 27.5 1.0 OD2 B:ASP369 2.4 27.4 1.0 NE2 B:HIS370 3.0 25.3 1.0 CG B:ASN51 3.1 27.6 1.0 CB B:SER102 3.1 17.9 1.0 ND1 B:HIS370 3.1 30.4 1.0 CG B:ASP369 3.2 24.5 1.0 ND2 B:ASN51 3.3 30.6 1.0 OD1 B:ASP369 3.4 25.7 1.0 O4 B:PO4453 3.8 39.4 0.8 CA B:SER102 3.8 18.1 1.0 CG B:ASP327 4.0 33.2 1.0 CD2 B:HIS370 4.0 18.5 1.0 OD1 B:ASP327 4.0 35.9 1.0 ZN B:ZN450 4.0 36.2 0.9 OD2 B:ASP327 4.1 35.2 1.0 CG B:HIS370 4.1 22.3 1.0 O1 B:PO4453 4.1 35.5 0.8 N B:SER102 4.1 12.8 1.0 O2 B:PO4453 4.2 34.3 0.8 P B:PO4453 4.2 37.4 0.8 CB B:ASN51 4.5 18.2 1.0 N B:GLY52 4.5 11.2 1.0 O B:HOH506 4.5 55.2 1.0 CB B:ASP327 4.5 28.1 1.0 CB B:ASP369 4.5 17.2 1.0 NE2 B:HIS412 4.7 38.9 1.0 O B:HOH572 4.8 39.1 1.0 CA B:ASN51 4.8 12.7 1.0 C B:ASN51 4.8 13.6 1.0 CE1 B:HIS412 4.8 35.5 1.0

T.T.Tibbitts, J.E.Murphy, E.R.Kantrowitz. Kinetic and Structural Consequences of Replacing the Aspartate Bridge By Asparagine in the Catalytic Metal Triad of Escherichia Coli Alkaline Phosphatase. J.Mol.Biol. V. 257 700 1996.
ISSN: ISSN 0022-2836
PubMed: 8648634
DOI: 10.1006/JMBI.1996.0195