Sodium in PDB 6bwl: X-Ray Structure of Pal From Bacillus Thuringiensis

All present enzymatic activity of X-Ray Structure of Pal From Bacillus Thuringiensis:
4.2.1.46;

The structure of X-Ray Structure of Pal From Bacillus Thuringiensis, PDB code: 6bwl was solved by N.A.Delvaux, J.B.Thoden, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.50 / 1.45
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	96.420, 98.341, 98.603, 90.00, 90.00, 90.00
R / Rfree (%)	12.9 / 15.1

The structure of X-Ray Structure of Pal From Bacillus Thuringiensis also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Sodium atom in the X-Ray Structure of Pal From Bacillus Thuringiensis (pdb code 6bwl). 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 X-Ray Structure of Pal From Bacillus Thuringiensis, PDB code: 6bwl:

Sodium binding site 1 out of 1 in the X-Ray Structure of Pal From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Structure of Pal From Bacillus Thuringiensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Na409 b:26.0 occ:1.00 OD2 A:ASP247 2.3 15.6 1.0 O A:HOH877 2.3 38.5 1.0 O A:HOH904 2.4 36.7 1.0 O A:HOH689 2.4 21.2 1.0 O A:HOH874 2.5 28.4 1.0 O A:ASP247 2.5 13.5 1.0 C A:ASP247 3.3 12.2 1.0 CG A:ASP247 3.5 13.0 1.0 O A:HOH713 3.7 33.5 1.0 N A:ASP247 3.7 11.2 1.0 CA A:ASP247 3.9 11.4 1.0 O A:HOH661 4.1 29.0 1.0 CB A:ASP247 4.2 11.6 1.0 N A:ILE248 4.3 10.7 1.0 OD1 A:ASP247 4.4 13.9 1.0 O A:HOH988 4.4 30.1 1.0 O A:HOH806 4.6 16.6 1.0 CA A:ILE248 4.6 11.1 1.0 O A:HOH1030 4.9 26.2 1.0 NE2 A:GLN246 4.9 29.0 0.5 C A:GLN246 4.9 12.8 1.0

N.A.Delvaux, J.B.Thoden, H.M.Holden. Molecular Architectures of Pen and Pal: Key Enzymes Required For Cmp-Pseudaminic Acid Biosynthesis in Bacillus Thuringiensis. Protein Sci. V. 27 738 2018.
ISSN: ESSN 1469-896X
PubMed: 29266550
DOI: 10.1002/PRO.3368