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

Enzymatic activity of 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;

Protein crystallography data

The structure of A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability, PDB code: 7qop 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) 75.31 / 1.80
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 106.499, 106.499, 83.006, 90, 90, 90
R / Rfree (%) 17.8 / 21.7

Other elements in 7qop:

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

Magnesium Binding Sites:

The binding sites of Magnesium atom in the A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability (pdb code 7qop). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the A Mutant of the Nitrile Hydratase From Geobacillus Pallidus Having Enhanced Thermostability, PDB code: 7qop:

Magnesium binding site 1 out of 1 in 7qop

Go back to Magnesium Binding Sites List in 7qop
Magnesium binding site 1 out of 1 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:22.7
occ:1.00
 OD1 B:ASP218 2.8 20.9 1.0
O A:ILE173 2.8 15.4 1.0
N A:SER171 2.9 14.3 1.0
OG A:SER171 3.1 12.7 1.0
C A:SER169 3.2 14.5 1.0
CA A:SER169 3.2 13.2 1.0
N A:SER170 3.2 14.3 1.0
O A:SER171 3.4 14.2 1.0
C A:SER171 3.6 16.1 1.0
CG B:ASP218 3.6 17.1 1.0
CA A:SER171 3.6 14.5 1.0
C A:ILE173 3.7 12.9 1.0
CE1 A:PHE175 3.8 16.7 1.0
CB A:SER171 3.8 14.7 1.0
O A:SER169 3.8 17.4 1.0
N A:ILE173 3.9 12.5 1.0
CB A:ILE173 3.9 12.9 1.0
C A:SER170 3.9 14.4 1.0
CB A:SER169 4.0 15.0 1.0
O A:ASP168 4.0 13.3 1.0
CA A:SER170 4.1 14.1 1.0
CA A:ILE173 4.1 13.9 1.0
CB B:ASP218 4.1 14.2 1.0
NH1 A:ARG174 4.2 15.9 1.0
N A:SER169 4.3 11.8 1.0
CZ A:PHE175 4.4 15.3 1.0
N A:GLU172 4.5 14.1 1.0
OG A:SER170 4.5 14.1 1.0
OD2 B:ASP218 4.6 14.6 1.0
C A:ASP168 4.6 12.3 1.0
OG A:SER169 4.6 15.9 1.0
CD1 A:PHE175 4.7 15.6 1.0
C A:GLU172 4.7 14.1 1.0
CG2 A:ILE173 4.8 12.8 1.0
N A:ARG174 4.9 14.7 1.0
CG1 A:ILE173 4.9 12.5 1.0
CB A:SER170 5.0 14.5 1.0

Reference:

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.
Page generated: Thu Oct 3 05:14:48 2024

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