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Sodium in PDB 7bgw: 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011

Enzymatic activity of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011

All present enzymatic activity of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011:
5.2.1.8;

Protein crystallography data

The structure of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011, PDB code: 7bgw 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) 34.42 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.455, 111.794, 62.559, 90, 90, 90
R / Rfree (%) 17.2 / 20.3

Other elements in 7bgw:

The structure of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011 (pdb code 7bgw). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011, PDB code: 7bgw:

Sodium binding site 1 out of 1 in 7bgw

Go back to Sodium Binding Sites List in 7bgw
Sodium binding site 1 out of 1 in the 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of 14-3-3 Sigma with PIN1 Binding Site PS72 and Covalently Bound LVD1011 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na305

b:29.3
occ:0.92
 OG A:SER64 2.6 30.6 1.0
O A:HOH589 2.8 27.3 1.0
C A:SER64 3.7 18.6 1.0
N A:ILE65 3.7 14.0 1.0
CB A:SER64 3.7 15.7 1.0
O A:SER64 3.8 17.6 1.0
CG1 A:ILE65 3.8 12.0 1.0
CA A:ILE65 3.9 15.9 1.0
CA A:SER64 4.3 13.6 1.0
CB A:ILE65 4.5 17.7 1.0
O A:VAL61 4.7 10.4 1.0
O A:HOH703 4.8 37.2 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: Tue Oct 8 16:12:38 2024

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