Sodium in PDB 7aaw: Thioredoxin Reductase From Bacillus Cereus

All present enzymatic activity of Thioredoxin Reductase From Bacillus Cereus:
1.8.1.9;

The structure of Thioredoxin Reductase From Bacillus Cereus, PDB code: 7aaw was solved by M.Shoor, I.Gudim, H.-P.Hersleth, M.Hammerstad, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.72 / 2.25
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	94.98, 94.98, 214.622, 90, 90, 90
R / Rfree (%)	17.9 / 21.9

The binding sites of Sodium atom in the Thioredoxin Reductase From Bacillus Cereus (pdb code 7aaw). 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 Thioredoxin Reductase From Bacillus Cereus, PDB code: 7aaw:

Sodium binding site 1 out of 1 in the Thioredoxin Reductase From Bacillus Cereus


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Thioredoxin Reductase From Bacillus Cereus within 5.0Å range: probe atom residue distance (Å) B Occ B:Na404 b:47.1 occ:1.00 O B:HOH583 2.3 54.1 1.0 O B:HOH584 2.3 48.3 1.0 O B:VAL199 2.4 48.2 1.0 O B:ASN196 2.5 44.3 1.0 O B:PHE194 2.7 45.2 1.0 O B:ALA193 2.7 43.2 1.0 C B:PHE194 3.3 44.8 1.0 C B:VAL199 3.5 46.1 1.0 C B:ASN196 3.6 41.7 1.0 CA B:PHE194 3.7 44.3 1.0 C B:ALA193 3.8 44.5 1.0 N B:ASN196 3.9 44.1 1.0 CB B:VAL199 4.0 46.2 1.0 CA B:VAL199 4.1 40.4 1.0 N B:VAL199 4.2 44.4 1.0 N B:GLN195 4.2 43.9 1.0 N B:PHE194 4.2 45.8 1.0 CA B:ASN196 4.3 42.4 1.0 C B:GLN195 4.5 46.9 1.0 N B:ASP200 4.5 44.7 1.0 N B:GLU197 4.6 46.7 1.0 CG1 B:VAL199 4.7 37.2 1.0 CA B:ASP200 4.7 48.8 1.0 CA B:GLN195 4.7 47.1 1.0 CB B:ASN196 4.7 45.6 1.0 CA B:GLU197 4.8 52.6 1.0 C B:GLU197 4.8 50.5 1.0 CE1 B:PHE201 5.0 44.5 1.0

M.Shoor, I.Gudim, H.P.Hersleth, M.Hammerstad. Thioredoxin Reductase From Bacillus Cereus Exhibits Distinct Reduction and Nadph-Binding Properties. Febs Open Bio 2021.
ISSN: ESSN 2211-5463
PubMed: 34492167
DOI: 10.1002/2211-5463.13289