Magnesium in PDB 1ipw: Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions

All present enzymatic activity of Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions:
3.6.1.1;

The structure of Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions, PDB code: 1ipw was solved by J.A.Kankare, A.Goldman, 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	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	109.400, 109.400, 154.300, 90.00, 90.00, 120.00
R / Rfree (%)	17.1 / 23.9

The binding sites of Magnesium atom in the Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions (pdb code 1ipw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions, PDB code: 1ipw:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg176 b:36.3 occ:0.50 O A:HOH230 1.7 38.7 1.0 O A:HOH209 1.8 39.8 1.0 OD2 A:ASP65 2.0 55.6 1.0 OD1 A:ASP102 2.3 43.6 1.0 CG A:ASP65 2.9 53.9 1.0 OD2 A:ASP70 3.2 41.2 1.0 CG A:ASP102 3.3 39.9 1.0 OD1 A:ASP65 3.4 60.1 1.0 OD2 A:ASP102 3.6 39.2 1.0 OG A:SER63 4.0 46.0 1.0 CG A:ASP70 4.0 30.6 1.0 CB A:ASP65 4.2 50.4 1.0 O A:ALA103 4.3 31.7 1.0 O A:HOH231 4.3 57.1 1.0 OD1 A:ASP70 4.4 36.8 1.0 NZ A:LYS104 4.4 27.0 1.0 CB A:ASP102 4.6 36.8 1.0 O A:PRO68 4.7 25.8 1.0 N A:ALA103 4.7 32.3 1.0 CA A:ASP102 4.9 36.8 1.0

Magnesium binding site 2 out of 3 in the Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg176 b:21.8 occ:0.50 O B:HOH232 1.7 36.2 1.0 O B:HOH188 1.8 29.7 1.0 OD2 B:ASP65 1.8 47.5 1.0 O B:HOH233 2.1 63.2 1.0 OD1 B:ASP102 2.2 34.6 1.0 O B:HOH229 2.6 61.9 1.0 CG B:ASP65 2.7 42.8 1.0 OD1 B:ASP65 2.9 43.9 1.0 CG B:ASP102 3.3 32.3 1.0 OD2 B:ASP70 3.5 32.4 1.0 OG B:SER63 3.7 42.8 1.0 O B:HOH222 3.9 44.5 1.0 OD2 B:ASP102 3.9 27.5 1.0 CB B:ASP65 4.1 42.9 1.0 O B:ALA103 4.1 29.1 1.0 N B:ALA103 4.4 27.4 1.0 CG B:ASP70 4.4 23.9 1.0 CB B:ASP102 4.5 30.1 1.0 CA B:ASP102 4.5 28.6 1.0 O B:PRO68 4.6 23.3 1.0 CB B:SER63 4.7 34.4 1.0

Magnesium binding site 3 out of 3 in the Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Inorganic Pyrophosphatase From Escherichia Coli with Three Magnesium Ions within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg177 b:29.5 occ:1.00 O A:HOH229 1.8 30.5 1.0 O B:HOH227 1.9 25.9 1.0 O B:HOH228 2.0 27.2 1.0 O B:HOH226 2.0 24.1 1.0 O A:HOH228 2.1 18.3 1.0 O A:HOH224 2.7 28.2 1.0 OD1 B:ASN24 3.7 21.7 1.0 OD1 A:ASN24 3.8 21.9 1.0 O B:ALA25 3.9 13.6 1.0 O B:ASN24 4.1 22.6 1.0 O A:ALA25 4.2 13.0 1.0 C B:ALA25 4.3 10.7 1.0 O A:ASN24 4.4 17.8 1.0 CG B:ASN24 4.4 19.7 1.0 C B:ASN24 4.5 17.3 1.0 C A:ALA25 4.5 10.9 1.0 OD1 A:ASP26 4.6 13.7 1.0 CG A:ASN24 4.6 18.7 1.0 OD1 B:ASP26 4.6 14.9 1.0 CA B:ALA25 4.7 13.8 1.0 N B:ALA25 4.7 17.7 1.0 C A:ASN24 4.7 14.9 1.0 ND2 B:ASN24 4.8 21.1 1.0 N B:ASP26 4.8 12.2 1.0 CA A:ALA25 4.9 12.3 1.0 ND2 A:ASN24 4.9 21.3 1.0 N A:ASP26 4.9 8.6 1.0 CD2 B:PHE50 4.9 14.4 1.0 N A:ALA25 5.0 14.4 1.0

J.Kankare, T.Salminen, R.Lahti, B.S.Cooperman, A.A.Baykov, A.Goldman. Crystallographic Identification of Metal-Binding Sites in Escherichia Coli Inorganic Pyrophosphatase. Biochemistry V. 35 4670 1996.
ISSN: ISSN 0006-2960
PubMed: 8664256
DOI: 10.1021/BI952637E