Sodium in PDB 3nys: X-Ray Structure of the K185A Mutant of Wbpe (Wlbe) From Pseudomonas Aeruginosa in Complex with Plp at 1.45 Angstrom Resolution

The structure of X-Ray Structure of the K185A Mutant of Wbpe (Wlbe) From Pseudomonas Aeruginosa in Complex with Plp at 1.45 Angstrom Resolution, PDB code: 3nys was solved by H.M.Holden, J.B.Thoden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.45
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	56.783, 93.570, 77.067, 90.00, 115.58, 90.00
R / Rfree (%)	17 / 20.1

The binding sites of Sodium atom in the X-Ray Structure of the K185A Mutant of Wbpe (Wlbe) From Pseudomonas Aeruginosa in Complex with Plp at 1.45 Angstrom Resolution (pdb code 3nys). 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 the K185A Mutant of Wbpe (Wlbe) From Pseudomonas Aeruginosa in Complex with Plp at 1.45 Angstrom Resolution, PDB code: 3nys:

Sodium binding site 1 out of 1 in the X-Ray Structure of the K185A Mutant of Wbpe (Wlbe) From Pseudomonas Aeruginosa in Complex with Plp at 1.45 Angstrom Resolution


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 the K185A Mutant of Wbpe (Wlbe) From Pseudomonas Aeruginosa in Complex with Plp at 1.45 Angstrom Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Na369 b:5.8 occ:0.50 O A:HOH592 2.1 5.4 1.0 O A:HOH564 2.1 6.8 1.0 O A:HOH818 2.1 6.8 1.0 OD2 A:ASP231 4.0 6.7 1.0 O A:HOH499 4.0 7.7 1.0 O A:ASP192 4.2 7.9 1.0 OD1 A:ASP231 4.2 6.4 1.0 O A:HOH490 4.2 7.4 1.0 CG A:ASP231 4.4 5.3 1.0 O A:ALA57 4.7 6.1 1.0 CB A:ASP192 4.7 5.9 1.0 O A:ARG229 4.7 6.8 1.0 CB A:ALA57 5.0 6.2 1.0 C A:ASP192 5.0 7.3 1.0

G.T.Dow, M.Gilbert, J.B.Thoden, H.M.Holden. Structural Investigation on Wlarg From Campylobacter Jejuni: A Sugar Aminotransferase. Protein Sci. V. 26 586 2017.
ISSN: ISSN 0961-8368
PubMed: 28028852
DOI: 10.1002/PRO.3109