Magnesium in PDB 7qou: A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability

All present enzymatic activity of A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability:
4.2.1.84;

The structure of A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability, PDB code: 7qou was solved by J.C.Van Wyk, D.A.Cowan, M.J.Danson, T.L.Tsekoa, M.F.Sayed, B.T.Sewell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	74.95 / 1.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	106.084, 106.084, 82.975, 90, 90, 90
R / Rfree (%)	15.3 / 18.2

The structure of A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Cobalt	(Co)	1 atom

The binding sites of Magnesium atom in the A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability (pdb code 7qou). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability, PDB code: 7qou:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:17.0 occ:1.00 OD1 B:ASP218 2.8 12.1 1.0 O A:ILE173 2.8 9.7 1.0 N A:SER171 2.9 9.3 1.0 OG A:SER171 3.2 9.9 1.0 CA A:SER169 3.2 9.8 1.0 C A:SER169 3.2 9.8 1.0 N A:SER170 3.2 9.2 1.0 O A:SER171 3.3 10.3 1.0 CA A:SER171 3.6 8.4 1.0 CG B:ASP218 3.6 11.4 1.0 C A:SER171 3.6 9.5 1.0 C A:ILE173 3.7 9.8 1.0 CE1 A:PHE175 3.8 11.4 1.0 CB A:SER171 3.8 9.7 1.0 O A:SER169 3.9 11.8 1.0 N A:ILE173 3.9 9.4 1.0 CB A:ILE173 3.9 9.7 1.0 C A:SER170 3.9 8.7 1.0 O A:ASP168 4.0 9.9 1.0 CB A:SER169 4.0 10.5 1.0 CA A:ILE173 4.1 10.0 1.0 CB B:ASP218 4.1 9.3 1.0 CA A:SER170 4.1 8.6 1.0 NH1 A:ARG174 4.2 11.7 1.0 N A:SER169 4.3 8.4 1.0 CZ A:PHE175 4.4 11.6 1.0 OG A:SER170 4.5 10.2 1.0 N A:GLU172 4.5 9.4 1.0 OD2 B:ASP218 4.5 10.1 1.0 C A:ASP168 4.6 7.8 1.0 OG A:SER169 4.7 13.6 1.0 C A:GLU172 4.7 9.6 1.0 CD1 A:PHE175 4.7 10.9 1.0 CG2 A:ILE173 4.8 11.1 1.0 N A:ARG174 4.9 10.4 1.0 CG1 A:ILE173 4.9 10.1 1.0 CB A:SER170 5.0 10.2 1.0

Magnesium binding site 2 out of 2 in the A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:36.4 occ:1.00 OD2 A:ASP108 4.0 11.8 1.0 OD1 A:ASP108 4.0 12.7 1.0 OE2 A:GLU183 4.1 49.6 1.0 CG A:ASP108 4.5 11.5 1.0 NE2 A:GLN180 4.8 13.1 1.0

J.C.Van Wyk, D.A.Cowan, M.J.Danson, T.L.Tsekoa, M.F.Sayed, B.T.Sewell. A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability To Be Published.