Magnesium in PDB 7nix: 14-3-3 Sigma with AS160 Binding Site PT642

Protein crystallography data

The structure of 14-3-3 Sigma with AS160 Binding Site PT642, PDB code: 7nix was solved by M.Wolter, C.Ottmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.61 / 1.90
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 121.219, 121.219, 74.464, 90, 90, 120
R / Rfree (%) 18.6 / 20.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the 14-3-3 Sigma with AS160 Binding Site PT642 (pdb code 7nix). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the 14-3-3 Sigma with AS160 Binding Site PT642, PDB code: 7nix:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 7nix

Go back to Magnesium Binding Sites List in 7nix
Magnesium binding site 1 out of 2 in the 14-3-3 Sigma with AS160 Binding Site PT642


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 AS160 Binding Site PT642 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg303

b:38.4
occ:0.81
O A:HOH575 2.2 51.1 1.0
O A:HOH563 2.4 47.6 1.0
O A:HOH431 2.4 39.4 1.0
O A:HOH513 2.5 29.6 1.0
O A:HOH459 2.6 28.5 1.0
O A:HOH564 3.6 39.1 0.4
O A:HOH406 4.0 41.5 1.0
O1 A:NHE301 4.2 39.7 1.0
O A:GLU17 4.3 24.1 1.0
O A:HOH536 4.4 38.3 1.0
O A:HOH454 4.5 24.6 1.0
O A:HOH496 4.5 26.7 1.0

Magnesium binding site 2 out of 2 in 7nix

Go back to Magnesium Binding Sites List in 7nix
Magnesium binding site 2 out of 2 in the 14-3-3 Sigma with AS160 Binding Site PT642


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of 14-3-3 Sigma with AS160 Binding Site PT642 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg304

b:51.6
occ:1.00
O A:HOH521 2.2 44.4 1.0
OE2 A:GLU89 2.4 39.6 1.0
O A:HOH444 2.4 47.3 1.0
CD A:GLU89 3.4 35.1 1.0
HG2 A:GLU89 3.7 35.9 1.0
HH12 A:ARG85 3.7 51.3 1.0
O A:HOH533 3.8 57.8 1.0
O A:HOH489 4.0 40.2 1.0
HG2 A:GLU86 4.0 48.1 1.0
CG A:GLU89 4.0 29.9 1.0
HB3 A:GLU89 4.0 36.0 1.0
HE22 A:GLN93 4.1 41.3 1.0
HH11 A:ARG85 4.1 51.3 1.0
NH1 A:ARG85 4.2 42.8 1.0
OE1 A:GLU89 4.3 26.0 1.0
HA A:GLU86 4.3 34.4 1.0
HG1 A:THR90 4.5 36.9 1.0
HB3 A:GLU86 4.6 38.7 1.0
CB A:GLU89 4.6 30.0 1.0
NE2 A:GLN93 4.8 34.4 1.0
OG1 A:THR90 4.8 30.8 1.0
OE1 A:GLN93 4.8 33.1 1.0
HG3 A:GLU89 4.9 35.9 1.0
CG A:GLU86 4.9 40.1 1.0
O A:GLU86 4.9 28.8 1.0

Reference:

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
Page generated: Mon Jul 12 14:40:24 2021

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