Magnesium in PDB 3lgy: R178A Mutant of the Degs-Deltapdz Protease

The structure of R178A Mutant of the Degs-Deltapdz Protease, PDB code: 3lgy was solved by J.Sohn, R.A.Grant, R.T.Sauer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.46 / 2.70
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	70.216, 70.216, 119.228, 90.00, 90.00, 120.00
R / Rfree (%)	23.6 / 25.2

The structure of R178A Mutant of the Degs-Deltapdz Protease also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the R178A Mutant of the Degs-Deltapdz Protease (pdb code 3lgy). 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 R178A Mutant of the Degs-Deltapdz Protease, PDB code: 3lgy:

Magnesium binding site 1 out of 1 in the R178A Mutant of the Degs-Deltapdz Protease


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of R178A Mutant of the Degs-Deltapdz Protease within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg257 b:90.1 occ:1.00 CL A:CL1 2.5 66.2 0.3 O A:ASP193 2.7 55.8 1.0 O A:GLN170 2.9 57.5 1.0 HA A:ALA194 3.1 86.8 1.0 O A:HOH11 3.1 53.6 1.0 H A:SER195 3.6 0.8 1.0 C A:ASP193 3.7 67.2 1.0 CA A:ALA194 4.0 72.4 1.0 C A:GLN170 4.1 51.4 1.0 N A:SER195 4.2 89.0 1.0 HA2 A:GLY171 4.2 74.3 1.0 N A:ALA194 4.2 74.2 1.0 HA3 A:GLY171 4.3 74.3 1.0 HB2 A:ASP193 4.5 67.0 1.0 HB3 A:SER195 4.5 0.3 1.0 C A:ALA194 4.6 70.5 1.0 H A:GLN170 4.6 71.4 1.0 CA A:GLY171 4.6 62.0 1.0 HB A:THR169 4.7 79.7 1.0 N A:GLY171 4.9 57.6 1.0 CG A:ASP193 4.9 62.5 1.0 OD1 A:ASP193 4.9 65.7 1.0 CB A:ASP193 5.0 55.8 1.0 CA A:ASP193 5.0 76.1 1.0

J.Sohn, R.A.Grant, R.T.Sauer. Allostery Is An Intrinsic Property of the Protease Domain of Degs: Implications For Enzyme Function and Evolution. J.Biol.Chem. V. 285 34039 2010.
ISSN: ISSN 0021-9258
PubMed: 20739286
DOI: 10.1074/JBC.M110.135541