Magnesium in PDB 3zqi: Structure of Tetracycline Repressor in Complex with Inducer Peptide- TIP2

The structure of Structure of Tetracycline Repressor in Complex with Inducer Peptide- TIP2, PDB code: 3zqi was solved by M.Sevvana, D.Goeke, C.Stoeckle, D.Kaspar, S.Grubmueller, C.Goetz, C.Wimmer, C.Berens, M.Klotzsche, Y.A.Muller, W.Hillen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.88 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.700, 78.560, 103.880, 90.00, 90.00, 90.00
R / Rfree (%)	16 / 19.5

The binding sites of Magnesium atom in the Structure of Tetracycline Repressor in Complex with Inducer Peptide- TIP2 (pdb code 3zqi). 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 Structure of Tetracycline Repressor in Complex with Inducer Peptide- TIP2, PDB code: 3zqi:

Magnesium binding site 1 out of 1 in the Structure of Tetracycline Repressor in Complex with Inducer Peptide- TIP2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Tetracycline Repressor in Complex with Inducer Peptide- TIP2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1207 b:23.1 occ:1.00 O A:HOH2032 2.0 26.7 1.0 O D:HOH2006 2.0 23.0 1.0 O A:HOH2123 2.1 19.9 1.0 O A:HOH2160 2.1 25.1 1.0 O A:HOH2033 2.2 20.0 1.0 O D:HOH2005 2.3 25.2 1.0 OE1 A:GLU23 3.9 31.0 1.0 O A:HOH2034 4.2 37.7 1.0 O A:HOH2119 4.2 16.9 1.0 OE2 A:GLU150 4.2 22.3 1.0 OE2 A:GLU23 4.2 31.1 1.0 OD1 A:ASP95 4.3 16.2 1.0 O A:HOH2170 4.3 32.7 1.0 OD2 A:ASP95 4.3 15.4 1.0 O A:HOH2011 4.3 36.2 1.0 OE1 A:GLU150 4.3 23.2 1.0 NZ A:LYS98 4.3 19.4 1.0 CD A:GLU23 4.5 29.4 1.0 CG A:ASP95 4.7 16.0 1.0 CD A:GLU150 4.7 19.2 1.0 CG1 A:VAL153 4.9 18.3 1.0

M.Sevvana, C.Goetz, D.Goeke, C.Wimmer, C.Berens, W.Hillen, Y.A.Muller. An Exclusive Alpha/Beta Code Directs Allostery in Tetr-Peptide Complexes. J.Mol.Biol. V. 416 46 2012.
ISSN: ISSN 0022-2836
PubMed: 22178479
DOI: 10.1016/J.JMB.2011.12.008