Sodium in PDB 5jda: Bacillus Cereus Coth Kinase Plus MG2+/Amp

All present enzymatic activity of Bacillus Cereus Coth Kinase Plus MG2+/Amp:
2.7.11.1;

The structure of Bacillus Cereus Coth Kinase Plus MG2+/Amp, PDB code: 5jda was solved by D.R.Tomchick, V.S.Tagliabracci, A.Sreelatha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.28 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.757, 63.516, 118.284, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 18.4

The structure of Bacillus Cereus Coth Kinase Plus MG2+/Amp also contains other interesting chemical elements:

Magnesium

(Mg)

5 atoms

The binding sites of Sodium atom in the Bacillus Cereus Coth Kinase Plus MG2+/Amp (pdb code 5jda). 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 Bacillus Cereus Coth Kinase Plus MG2+/Amp, PDB code: 5jda:

Sodium binding site 1 out of 1 in the Bacillus Cereus Coth Kinase Plus MG2+/Amp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Bacillus Cereus Coth Kinase Plus MG2+/Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Na407 b:44.5 occ:1.00 O A:HOH567 2.3 46.6 1.0 H5'2 A:AMP401 2.5 41.9 1.0 O1P A:AMP401 2.6 32.2 1.0 HE2 A:HIS227 2.6 31.2 1.0 H5'1 A:AMP401 2.8 41.9 1.0 C5' A:AMP401 3.0 34.9 1.0 P A:AMP401 3.2 33.7 1.0 O2P A:AMP401 3.2 39.0 1.0 O5' A:AMP401 3.3 36.1 1.0 NE2 A:HIS227 3.4 26.0 1.0 O A:HOH620 3.5 37.9 1.0 O A:HOH563 3.7 24.8 1.0 HE1 A:HIS227 3.9 37.1 1.0 CE1 A:HIS227 4.0 30.9 1.0 O A:HOH547 4.2 21.6 1.0 O A:HOH734 4.3 33.7 1.0 C4' A:AMP401 4.4 26.4 1.0 H3' A:AMP401 4.5 28.9 1.0 CD2 A:HIS227 4.6 24.3 1.0 O3P A:AMP401 4.7 31.4 1.0 OD2 A:ASP246 4.7 26.5 1.0 HD2 A:HIS227 4.8 29.2 1.0

K.B.Nguyen, A.Sreelatha, E.S.Durrant, J.Lopez-Garrido, A.Muszewska, M.Dudkiewicz, M.Grynberg, S.Yee, K.Pogliano, D.R.Tomchick, K.Pawowski, J.E.Dixon, V.S.Tagliabracci. Phosphorylation of Spore Coat Proteins By A Family of Atypical Protein Kinases. Proc.Natl.Acad.Sci.Usa V. 113 E3482 2016.
ISSN: ESSN 1091-6490
PubMed: 27185916
DOI: 10.1073/PNAS.1605917113