Magnesium in PDB 7nrl: 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1032

All present enzymatic activity of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1032:
5.2.1.8;

The structure of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1032, PDB code: 7nrl was solved by M.Wolter, L.V.Dijck, P.J.Cossar, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.29 / 1.80
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.577, 112.599, 62.595, 90, 90, 90
R / Rfree (%)	18.6 / 22.5

The binding sites of Magnesium atom in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1032 (pdb code 7nrl). 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 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1032, PDB code: 7nrl:

Magnesium binding site 1 out of 1 in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1032


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1032 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg308 b:9.1 occ:1.00 O A:GLU110 2.3 10.5 1.0 OE2 A:GLU35 2.4 17.9 1.0 O A:HOH438 2.5 19.5 1.0 O A:HOH620 2.5 18.1 1.0 OE1 A:GLU35 2.6 18.8 1.0 CD A:GLU35 2.9 18.0 1.0 C A:GLU110 3.5 13.1 1.0 N A:GLY112 4.1 12.0 1.0 O A:HOH639 4.2 27.2 1.0 CG A:GLU35 4.3 15.8 1.0 CA A:GLU110 4.4 8.9 1.0 N A:ALA111 4.5 10.4 1.0 CB A:GLU110 4.5 14.7 1.0 CA A:ALA111 4.5 7.8 1.0 O A:HOH520 4.6 21.4 1.0 O A:HOH431 4.6 25.6 1.0 OE1 A:GLU110 4.7 22.7 1.0 C A:ALA111 4.7 14.5 1.0 O A:HOH514 4.8 19.2 1.0 CA A:GLY112 4.8 15.8 1.0

P.J.Cossar, M.Wolter, L.Van Dijck, D.Valenti, L.M.Levy, C.Ottmann, L.Brunsveld. Reversible Covalent Imine-Tethering For Selective Stabilization of 14-3-3 Hub Protein Interactions. J.Am.Chem.Soc. 2021.
ISSN: ESSN 1520-5126
PubMed: 34047554
DOI: 10.1021/JACS.1C03035