Magnesium in PDB 3olx: Structural and Functional Effects of Substitution at Position T+1 in Chey: CHEYA88S-BEF3-Mn Complex

The structure of Structural and Functional Effects of Substitution at Position T+1 in Chey: CHEYA88S-BEF3-Mn Complex, PDB code: 3olx was solved by R.M.Immormino, R.B.Bourret, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.88 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.687, 53.759, 160.013, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 23

The structure of Structural and Functional Effects of Substitution at Position T+1 in Chey: CHEYA88S-BEF3-Mn Complex also contains other interesting chemical elements:

Fluorine	(F)	9 atoms
Manganese	(Mn)	5 atoms

The binding sites of Magnesium atom in the Structural and Functional Effects of Substitution at Position T+1 in Chey: CHEYA88S-BEF3-Mn Complex (pdb code 3olx). 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 Structural and Functional Effects of Substitution at Position T+1 in Chey: CHEYA88S-BEF3-Mn Complex, PDB code: 3olx:

Magnesium binding site 1 out of 1 in the Structural and Functional Effects of Substitution at Position T+1 in Chey: CHEYA88S-BEF3-Mn Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural and Functional Effects of Substitution at Position T+1 in Chey: CHEYA88S-BEF3-Mn Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg134 b:42.9 occ:1.00 O B:HOH142 3.0 34.3 1.0 NZ A:LYS119 3.0 41.7 1.0 CB B:GLU93 3.2 46.1 1.0 NZ B:LYS92 3.2 33.9 1.0 O A:HOH152 3.2 33.8 1.0 CA B:GLU93 3.5 45.8 1.0 O B:HOH165 3.5 41.2 1.0 CE A:LYS119 3.7 46.9 1.0 N B:GLU93 3.9 34.9 1.0 CD A:LYS119 4.0 45.6 1.0 CD1 B:ILE96 4.2 36.9 1.0 O B:HOH239 4.4 48.1 1.0 CG B:GLU93 4.5 59.5 1.0 CG B:LYS92 4.5 40.3 1.0 CE B:LYS92 4.5 30.2 1.0 C B:LYS92 4.6 37.5 1.0 CE A:LYS122 4.6 45.6 1.0 O A:HOH181 4.6 54.1 1.0 CD A:LYS122 4.7 39.3 1.0 OE1 B:GLU93 4.7 71.3 1.0 O B:HOH161 4.8 39.5 1.0 CB B:LYS92 4.9 39.1 1.0 C B:GLU93 4.9 41.1 1.0 O A:TYR106 4.9 27.5 1.0 O B:HOH235 4.9 46.6 1.0 O A:HOH147 4.9 32.8 1.0 CD B:GLU93 5.0 73.6 1.0 O B:LYS92 5.0 35.8 1.0

R.M.Immormino, R.E.Silversmith, R.B.Bourret. A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation. Biochemistry V. 55 5595 2016.
ISSN: ISSN 0006-2960
PubMed: 27589219
DOI: 10.1021/ACS.BIOCHEM.6B00645