Sodium in PDB 6g6x: 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide

The structure of 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide, PDB code: 6g6x was solved by S.A.Andrei, V.Thijssen, L.Brunsveld, C.Ottmann, L.G.Milroy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.49 / 1.13
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.118, 111.849, 62.630, 90.00, 90.00, 90.00
R / Rfree (%)	15 / 16.8

The structure of 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Sodium atom in the 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide (pdb code 6g6x). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide, PDB code: 6g6x:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na305 b:18.2 occ:0.98 OE1 A:GLU75 2.4 47.2 1.0 O A:HOH489 2.5 29.8 1.0 CD A:GLU75 3.6 47.5 1.0 HB2 A:GLU75 3.8 57.1 1.0 HA A:GLU75 4.4 57.1 1.0 CB A:GLU75 4.5 47.6 1.0 OE2 A:GLU75 4.5 47.6 1.0 CG A:GLU75 4.5 47.5 1.0 HG2 A:GLU75 4.6 57.0 1.0 O A:GLY73 4.6 54.7 1.0 CA A:GLU75 4.9 47.6 1.0

Sodium binding site 2 out of 2 in the 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of 14-3-3SIGMA in Complex with A P129BETA3P Mutated Yap PS127 Phosphopeptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Na306 b:27.1 occ:0.91 O A:LYS77 2.4 31.6 1.0 OE1 A:GLU80 2.4 13.7 1.0 O A:HOH648 2.5 30.8 1.0 OE2 A:GLU80 2.8 15.9 1.0 CD A:GLU80 2.8 13.5 1.0 O A:HOH465 3.0 22.4 1.0 HA3 A:GLY78 3.2 23.5 1.0 C A:LYS77 3.5 31.1 1.0 CA A:GLY78 4.1 19.6 1.0 CG A:GLU80 4.1 11.8 1.0 HD2 A:PRO79 4.1 16.4 1.0 N A:GLY78 4.2 25.2 1.0 HG2 A:GLU80 4.2 14.2 1.0 HB2 A:GLU80 4.2 13.4 1.0 HB3 A:LYS77 4.3 46.1 1.0 HA A:LYS77 4.3 43.3 1.0 H A:GLU80 4.4 13.0 1.0 CA A:LYS77 4.4 36.1 1.0 C A:GLY78 4.7 15.7 1.0 CB A:GLU80 4.7 11.2 1.0 HA2 A:GLY78 4.8 23.5 1.0 HG3 A:GLU80 4.8 14.2 1.0 CB A:LYS77 4.9 38.4 1.0 CD A:PRO79 5.0 13.7 1.0

S.A.Andrei, V.Thijssen, L.Brunsveld, C.Ottmann, L.G.Milroy. A Study on the Effect of Synthetic Alpha-to-BETA3-Amino Acid Mutations on the Binding of Phosphopeptides to 14-3-3 Proteins. Chem.Commun.(Camb.) 2019.
ISSN: ESSN 1364-548X
PubMed: 31763628
DOI: 10.1039/C9CC07982C