Magnesium in PDB 6g60: Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline

All present enzymatic activity of Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline:
3.1.6.6;

The structure of Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline, PDB code: 6g60 was solved by S.Martinez-Rodriguez, A.Camara-Artigas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.18 / 1.84
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.538, 206.898, 116.602, 90.00, 110.17, 90.00
R / Rfree (%)	16.9 / 19.9

The binding sites of Magnesium atom in the Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline (pdb code 6g60). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline, PDB code: 6g60:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:32.2 occ:1.00 OD1 A:ASP14 2.1 29.1 1.0 NE2 A:HIS297 2.1 23.9 1.0 OD2 A:ASP296 2.1 26.1 1.0 OG2 A:DDZ54 2.3 36.1 1.0 CG A:ASP14 2.7 27.3 1.0 OD2 A:ASP14 2.7 31.9 1.0 CD2 A:HIS297 3.0 22.3 1.0 CG A:ASP296 3.0 24.5 1.0 CE1 A:HIS297 3.0 23.4 1.0 OD1 A:ASP296 3.2 22.1 1.0 CB A:DDZ54 3.4 34.2 1.0 CA A:DDZ54 3.6 25.7 1.0 OG1 A:DDZ54 3.6 30.7 1.0 NZ A:LYS102 3.9 31.3 1.0 CG A:HIS297 4.1 21.6 1.0 ND1 A:HIS297 4.1 22.6 1.0 N A:DDZ54 4.1 24.5 1.0 CB A:ASP14 4.1 22.6 1.0 CD2 A:HIS201 4.1 26.2 1.0 O A:HOH706 4.3 34.9 1.0 N A:GLN15 4.3 20.2 1.0 CB A:ASP296 4.4 19.6 1.0 NE A:ARG58 4.4 23.5 1.0 CA A:ASP14 4.5 21.6 1.0 NH2 A:ARG58 4.5 23.4 1.0 C A:ASP14 4.7 21.9 1.0 OE1 A:GLN15 4.8 22.5 1.0 NE2 A:HIS201 4.8 28.7 1.0 CB A:GLN15 4.9 21.0 1.0 CE A:LYS309 4.9 30.1 1.0 CA A:GLN15 4.9 22.6 1.0 C A:DDZ54 4.9 23.6 1.0 NZ A:LYS309 4.9 27.4 1.0 C A:LEU53 5.0 24.8 1.0 CZ A:ARG58 5.0 26.4 1.0

Magnesium binding site 2 out of 4 in the Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg602 b:31.8 occ:1.00 OD2 B:ASP296 2.0 21.9 1.0 OG2 B:DDZ54 2.0 33.6 1.0 NE2 B:HIS297 2.2 20.4 1.0 OD1 B:ASP14 2.2 25.2 1.0 OD2 B:ASP14 2.6 31.5 1.0 CG B:ASP14 2.7 26.0 1.0 CG B:ASP296 2.9 19.3 1.0 CD2 B:HIS297 3.0 18.9 1.0 CB B:DDZ54 3.1 29.6 1.0 CE1 B:HIS297 3.2 19.5 1.0 OD1 B:ASP296 3.2 18.4 1.0 OG1 B:DDZ54 3.5 31.6 1.0 CA B:DDZ54 3.5 18.9 1.0 N B:DDZ54 4.0 21.3 1.0 NZ B:LYS102 4.1 31.4 1.0 CG B:HIS297 4.1 17.2 1.0 O B:HOH760 4.2 32.3 1.0 ND1 B:HIS297 4.2 19.9 1.0 CB B:ASP14 4.2 18.8 1.0 CB B:ASP296 4.3 18.7 1.0 CD2 B:HIS201 4.3 25.1 1.0 NE B:ARG58 4.3 20.3 1.0 N B:GLN15 4.4 18.2 1.0 NH2 B:ARG58 4.5 21.5 1.0 CA B:ASP14 4.7 19.0 1.0 C B:DDZ54 4.8 15.7 1.0 CE B:LYS102 4.8 28.9 1.0 C B:ASP14 4.8 19.1 1.0 OE1 B:GLN15 4.9 21.5 1.0 C B:LEU53 4.9 19.1 1.0 CE B:LYS309 4.9 16.9 1.0 NE2 B:HIS201 4.9 26.2 1.0 CZ B:ARG58 4.9 22.1 1.0 NZ B:LYS309 5.0 16.8 1.0 CB B:GLN15 5.0 20.8 1.0

Magnesium binding site 3 out of 4 in the Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg602 b:34.6 occ:1.00 OG2 C:DDZ54 2.0 37.4 1.0 OD1 C:ASP14 2.2 36.5 1.0 NE2 C:HIS297 2.2 31.9 1.0 OD2 C:ASP296 2.2 36.5 1.0 OD2 C:ASP14 2.7 37.1 1.0 CG C:ASP14 2.8 34.7 1.0 CD2 C:HIS297 3.0 27.5 1.0 CG C:ASP296 3.1 29.4 1.0 CE1 C:HIS297 3.1 31.4 1.0 CB C:DDZ54 3.2 35.4 1.0 OD1 C:ASP296 3.5 25.5 1.0 CA C:DDZ54 3.5 29.4 1.0 OG1 C:DDZ54 3.6 39.2 1.0 NZ C:LYS102 4.0 39.0 1.0 N C:DDZ54 4.0 30.5 1.0 O C:HOH808 4.1 32.9 1.0 CG C:HIS297 4.2 29.3 1.0 ND1 C:HIS297 4.2 28.4 1.0 CD2 C:HIS201 4.2 32.5 1.0 CB C:ASP14 4.2 24.6 1.0 NE C:ARG58 4.3 27.5 1.0 CB C:ASP296 4.4 25.1 1.0 NH2 C:ARG58 4.5 30.9 1.0 N C:GLN15 4.5 26.9 1.0 CA C:ASP14 4.7 25.3 1.0 NZ C:LYS309 4.7 27.6 1.0 CE C:LYS102 4.7 36.4 1.0 C C:DDZ54 4.8 26.4 1.0 OE1 C:GLN15 4.8 28.9 1.0 NE2 C:HIS201 4.9 33.5 1.0 CZ C:ARG58 4.9 31.7 1.0 C C:LEU53 4.9 25.9 1.0 C C:ASP14 4.9 28.3 1.0 CE C:LYS309 4.9 27.1 1.0

Magnesium binding site 4 out of 4 in the Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Choline Sulfatase From Ensifer (Sinorhizobium) Meliloti Cocrystalized with Choline within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1001 b:49.0 occ:1.00 OG2 D:DDZ54 1.9 63.0 1.0 CE1 D:HIS297 2.4 31.4 1.0 OD2 D:ASP296 2.5 32.7 1.0 OD1 D:ASP14 2.5 42.9 1.0 CB D:DDZ54 2.8 48.1 1.0 OD2 D:ASP14 2.9 39.6 1.0 OG1 D:DDZ54 3.0 42.9 1.0 CG D:ASP14 3.1 38.0 1.0 CA D:DDZ54 3.2 35.3 1.0 NE2 D:HIS297 3.3 35.9 1.0 ND1 D:HIS297 3.4 34.6 1.0 CG D:ASP296 3.6 30.7 1.0 NZ D:LYS102 3.7 42.2 1.0 N D:DDZ54 3.8 30.6 1.0 O6 D:CHT1000 3.9 45.1 1.0 OD1 D:ASP296 4.0 27.0 1.0 CD2 D:HIS201 4.0 37.9 1.0 NE D:ARG58 4.4 28.7 1.0 CD2 D:HIS297 4.5 32.9 1.0 NZ D:LYS309 4.5 36.5 1.0 C D:DDZ54 4.5 28.2 1.0 CG D:HIS297 4.5 34.1 1.0 CB D:ASP14 4.6 33.1 1.0 CE D:LYS102 4.6 41.3 1.0 NE2 D:HIS201 4.6 38.8 1.0 CE D:LYS309 4.7 34.1 1.0 C D:LEU53 4.8 31.0 1.0 NH2 D:ARG58 4.8 29.0 1.0 CB D:ASP296 4.8 30.2 1.0 OE1 D:GLN15 4.9 32.4 1.0

S.Martinez-Rodriguez, A.Camara-Artigas. Structural Characterization of Choline-O-Sulfatase, A Member of the Promiscuous Alkaline Phosphatase Superfamily To Be Published.