Magnesium in PDB 1hjk: Alkaline Phosphatase Mutant H331Q

All present enzymatic activity of Alkaline Phosphatase Mutant H331Q:
3.1.3.1;

The structure of Alkaline Phosphatase Mutant H331Q, PDB code: 1hjk was solved by J.E.Murphy, B.Stec, L.Ma, E.R.Kantrowitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.30
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	195.520, 167.860, 77.030, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 20

The structure of Alkaline Phosphatase Mutant H331Q also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

The binding sites of Magnesium atom in the Alkaline Phosphatase Mutant H331Q (pdb code 1hjk). 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 H331Q, PDB code: 1hjk:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Alkaline Phosphatase Mutant H331Q


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 H331Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg452 b:9.1 occ:1.00 O A:HOH458 1.9 4.0 1.0 OG1 A:THR155 1.9 2.0 1.0 OD2 A:ASP51 2.1 5.2 1.0 OE2 A:GLU322 2.1 6.5 1.0 O A:HOH459 2.1 2.6 1.0 O A:HOH457 2.3 34.0 1.0 CB A:THR155 3.0 2.0 1.0 CD A:GLU322 3.1 9.2 1.0 CG A:ASP51 3.2 6.7 1.0 OE1 A:GLU322 3.4 2.0 1.0 OD2 A:ASP153 3.6 12.7 1.0 O A:HOH624 3.7 2.0 1.0 CB A:ASP51 3.8 4.9 1.0 CG2 A:THR155 3.9 2.0 1.0 N A:THR155 4.1 8.6 1.0 CA A:THR155 4.1 4.5 1.0 O A:HOH630 4.3 9.7 1.0 OD1 A:ASP51 4.3 2.0 1.0 O2P A:SEP102 4.3 32.5 1.0 CG A:GLU322 4.4 4.3 1.0 CB A:SEP102 4.7 5.5 1.0 CD A:PRO156 4.7 3.9 1.0 CB A:ALA324 4.8 2.0 1.0 CG A:ASP153 4.8 11.6 1.0 O A:ALA324 4.8 4.2 1.0 CA A:ALA324 4.8 4.9 1.0 ZN A:ZN451 5.0 11.1 1.0

Magnesium binding site 2 out of 2 in the Alkaline Phosphatase Mutant H331Q


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 H331Q within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg452 b:2.0 occ:1.00 O B:HOH459 2.0 14.3 1.0 OD2 B:ASP51 2.0 7.9 1.0 O B:HOH458 2.1 9.2 1.0 OG1 B:THR155 2.3 3.4 1.0 O B:HOH457 2.3 38.9 1.0 OE2 B:GLU322 2.5 10.8 1.0 OE1 B:GLU322 2.7 6.6 1.0 CD B:GLU322 3.0 7.7 1.0 CG B:ASP51 3.1 8.4 1.0 CB B:THR155 3.2 2.0 1.0 CB B:ASP51 3.7 2.0 1.0 OD2 B:ASP153 3.8 20.1 1.0 CG2 B:THR155 4.1 2.3 1.0 OD1 B:ASP51 4.1 2.0 1.0 N B:THR155 4.2 5.1 1.0 CA B:THR155 4.3 4.4 1.0 CG B:GLU322 4.4 2.5 1.0 CB B:ALA324 4.6 2.0 1.0 CA B:ALA324 4.6 3.4 1.0 O2P B:SEP102 4.7 32.5 1.0 O B:ALA324 4.7 6.9 1.0 CG B:ASP153 4.8 11.6 1.0 CD B:PRO156 4.8 6.7 1.0 CB B:SEP102 4.9 11.0 1.0

J.E.Murphy, B.Stec, L.Ma, E.R.Kantrowitz. Trapping and Visualization of A Covalent Enzyme-Phosphate Intermediate. Nat.Struct.Biol. V. 4 618 1997.
ISSN: ISSN 1072-8368
PubMed: 9253408
DOI: 10.1038/NSB0897-618