Magnesium in PDB 3qn3: Phosphopyruvate Hydratase From Campylobacter Jejuni.

All present enzymatic activity of Phosphopyruvate Hydratase From Campylobacter Jejuni.:
4.2.1.11;

The structure of Phosphopyruvate Hydratase From Campylobacter Jejuni., PDB code: 3qn3 was solved by J.Osipiuk, M.Gu, K.Kwon, W.F.Anderson, A.Joachimiak, Center For Structuralgenomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.90 / 2.13
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	120.470, 148.886, 234.719, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.6

The binding sites of Magnesium atom in the Phosphopyruvate Hydratase From Campylobacter Jejuni. (pdb code 3qn3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Phosphopyruvate Hydratase From Campylobacter Jejuni., PDB code: 3qn3:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Phosphopyruvate Hydratase From Campylobacter Jejuni.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphopyruvate Hydratase From Campylobacter Jejuni. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:33.9 occ:1.00 O A:HOH572 1.9 29.4 1.0 OD2 A:ASP307 2.0 33.9 1.0 OE2 A:GLU280 2.0 33.5 1.0 O A:HOH545 2.1 35.0 1.0 OD2 A:ASP239 2.1 37.0 1.0 O A:HOH467 2.1 27.6 1.0 CG A:ASP239 3.1 32.3 1.0 CG A:ASP307 3.1 33.5 1.0 CD A:GLU280 3.2 34.0 1.0 OD1 A:ASP239 3.4 30.4 1.0 CB A:ASP307 3.6 31.4 1.0 O A:HOH479 3.7 49.9 1.0 NZ A:LYS383 3.9 25.7 1.0 CG A:GLU280 4.0 32.2 1.0 OE1 A:GLN162 4.1 33.4 1.0 OE1 A:GLU280 4.1 32.8 1.0 OD1 A:ASP307 4.2 32.8 1.0 OE2 A:GLU163 4.2 37.5 1.0 CB A:ASP239 4.4 31.9 1.0 OD2 A:ASP281 4.4 33.4 1.0 NZ A:LYS332 4.4 31.7 1.0 CD2 A:LEU330 4.4 24.8 1.0 CD A:GLU163 4.9 37.9 1.0

Magnesium binding site 2 out of 4 in the Phosphopyruvate Hydratase From Campylobacter Jejuni.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Phosphopyruvate Hydratase From Campylobacter Jejuni. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:39.4 occ:1.00 O B:HOH416 2.0 34.7 1.0 OD2 B:ASP307 2.1 32.5 1.0 OD2 B:ASP239 2.1 30.8 1.0 O B:HOH452 2.1 35.1 1.0 OE2 B:GLU280 2.2 30.8 1.0 O B:HOH567 2.2 38.0 1.0 CG B:ASP239 3.1 33.9 1.0 CG B:ASP307 3.2 32.6 1.0 CD B:GLU280 3.4 34.6 1.0 OD1 B:ASP239 3.5 34.0 1.0 CB B:ASP307 3.8 33.2 1.0 NZ B:LYS383 3.9 35.0 1.0 NE2 B:GLN162 4.0 37.6 1.0 OE1 B:GLU280 4.2 30.7 1.0 OD2 B:ASP281 4.2 36.9 1.0 OD1 B:ASP307 4.3 31.0 1.0 OE2 B:GLU163 4.3 38.7 1.0 CG B:GLU280 4.3 30.7 1.0 CB B:ASP239 4.5 34.2 1.0 NZ B:LYS332 4.5 31.1 1.0 CD2 B:LEU330 4.5 27.9 1.0 CD B:GLU163 4.9 36.5 1.0

Magnesium binding site 3 out of 4 in the Phosphopyruvate Hydratase From Campylobacter Jejuni.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Phosphopyruvate Hydratase From Campylobacter Jejuni. within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:36.4 occ:1.00 OE2 C:GLU280 2.0 31.4 1.0 O C:HOH568 2.0 34.5 1.0 OD2 C:ASP307 2.0 28.8 1.0 O C:HOH446 2.1 29.2 1.0 O C:HOH544 2.1 32.2 1.0 OD2 C:ASP239 2.3 31.0 1.0 CG C:ASP307 3.1 29.3 1.0 CD C:GLU280 3.2 32.5 1.0 CG C:ASP239 3.2 30.4 1.0 OD1 C:ASP239 3.4 28.9 1.0 CB C:ASP307 3.6 29.2 1.0 NZ C:LYS383 3.9 32.4 1.0 CG C:GLU280 4.0 28.7 1.0 OE1 C:GLU280 4.1 31.4 1.0 NE2 C:GLN162 4.1 29.6 1.0 OD1 C:ASP307 4.2 31.6 1.0 OE2 C:GLU163 4.2 35.4 1.0 OD2 C:ASP281 4.3 31.4 1.0 O C:HOH587 4.3 51.7 1.0 CD2 C:LEU330 4.4 27.2 1.0 NZ C:LYS332 4.4 31.6 1.0 CB C:ASP239 4.6 29.1 1.0 O C:HOH432 4.6 56.0 1.0

Magnesium binding site 4 out of 4 in the Phosphopyruvate Hydratase From Campylobacter Jejuni.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Phosphopyruvate Hydratase From Campylobacter Jejuni. within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg601 b:33.6 occ:1.00 O D:HOH475 2.0 31.9 1.0 OD2 D:ASP307 2.0 35.2 1.0 O D:HOH439 2.1 30.0 1.0 O D:HOH459 2.1 43.0 1.0 OE2 D:GLU280 2.1 26.6 1.0 OD2 D:ASP239 2.1 31.6 1.0 CG D:ASP239 3.1 32.1 1.0 CG D:ASP307 3.1 33.1 1.0 CD D:GLU280 3.2 28.9 1.0 OD1 D:ASP239 3.4 31.1 1.0 CB D:ASP307 3.6 31.9 1.0 CG D:GLU280 4.0 27.9 1.0 NZ D:LYS383 4.1 26.3 1.0 OD1 D:ASP307 4.2 32.1 1.0 NE2 D:GLN162 4.2 30.2 1.0 OE1 D:GLU280 4.2 27.7 1.0 OE2 D:GLU163 4.2 32.7 1.0 NZ D:LYS332 4.3 34.1 1.0 OD2 D:ASP281 4.3 34.3 1.0 CB D:ASP239 4.4 29.5 1.0 CD2 D:LEU330 4.4 24.8 1.0 CD D:GLU163 4.9 33.5 1.0 CB D:ALA241 4.9 31.0 1.0

J.Osipiuk, M.Gu, K.Kwon, W.F.Anderson, A.Joachimiak. Phosphopyruvate Hydratase From Campylobacter Jejuni. To Be Published.