Sodium in PDB 6ghp: 14-3-3SIGMA in Complex with A TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac

The structure of 14-3-3SIGMA in Complex with A TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac, PDB code: 6ghp was solved by S.A.Andrei, P.J.De Vink, L.Brunsveld, C.Ottmann, Y.Higuchi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.61 / 1.95
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	82.453, 111.473, 63.675, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 23.1

The structure of 14-3-3SIGMA in Complex with A TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Sodium atom in the 14-3-3SIGMA in Complex with A TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac (pdb code 6ghp). 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 TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac, PDB code: 6ghp:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the 14-3-3SIGMA in Complex with A TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac


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 TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac within 5.0Å range: probe atom residue distance (Å) B Occ A:Na303 b:89.0 occ:1.00 OE2 A:GLU188 2.4 0.7 1.0 CD A:GLU188 3.3 0.9 1.0 HG2 A:GLU188 3.3 0.2 1.0 CG A:GLU188 3.8 98.5 1.0 OE1 A:GLU188 4.1 0.1 1.0 HG3 A:GLU188 4.3 0.2 1.0 O A:HOH442 4.9 42.2 1.0 HB3 A:GLU188 4.9 80.1 1.0

Sodium binding site 2 out of 2 in the 14-3-3SIGMA in Complex with A TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac


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 TASK3 Peptide Stabilized By Semi- Synthetic Natural Product Fc-Nac within 5.0Å range: probe atom residue distance (Å) B Occ A:Na304 b:48.9 occ:1.00 OXT A:THR231 2.3 42.5 1.0 O A:HOH567 2.4 76.2 1.0 O A:THR228 2.5 29.1 1.0 O A:HOH541 2.6 55.8 1.0 C A:THR231 3.5 41.6 1.0 HG21 A:THR228 3.6 46.8 1.0 C A:THR228 3.7 32.0 1.0 HG23 A:THR228 4.1 46.8 1.0 O A:THR231 4.1 47.6 1.0 HA A:THR228 4.1 33.0 1.0 H A:THR231 4.1 50.0 1.0 HA A:LEU229 4.3 33.0 1.0 CG2 A:THR228 4.3 39.0 1.0 CA A:THR228 4.5 27.5 1.0 N A:THR231 4.6 41.6 1.0 O A:LEU229 4.6 27.5 1.0 CA A:THR231 4.7 36.1 1.0 N A:LEU229 4.7 28.1 1.0 C A:LEU229 4.7 31.8 1.0 CA A:LEU229 4.8 27.5 1.0 HG1 A:THR231 4.9 51.1 1.0

S.A.Andrei, P.De Vink, E.Sijbesma, L.Han, L.Brunsveld, N.Kato, C.Ottmann, Y.Higuchi. Rationally Designed Semisynthetic Natural Product Analogues For Stabilization of 14-3-3 Protein-Protein Interactions. Angew. Chem. Int. Ed. Engl. V. 57 13470 2018.
ISSN: ESSN 1521-3773
PubMed: 30025189
DOI: 10.1002/ANIE.201806584