Chlorine in PDB 5u23: X-Ray Structure of the Wlarg Aminotransferase From Campylobacter Jejuni in Complex with Tdp-QUI3N

The structure of X-Ray Structure of the Wlarg Aminotransferase From Campylobacter Jejuni in Complex with Tdp-QUI3N, PDB code: 5u23 was solved by H.M.Holden, J.B.Thoden, G.T.Dow, M.Gilbert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.92 / 1.45
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	107.824, 56.644, 124.549, 90.00, 90.01, 90.00
R / Rfree (%)	12.7 / 15.3

The structure of X-Ray Structure of the Wlarg Aminotransferase From Campylobacter Jejuni in Complex with Tdp-QUI3N also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the X-Ray Structure of the Wlarg Aminotransferase From Campylobacter Jejuni in Complex with Tdp-QUI3N (pdb code 5u23). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the X-Ray Structure of the Wlarg Aminotransferase From Campylobacter Jejuni in Complex with Tdp-QUI3N, PDB code: 5u23:

Chlorine binding site 1 out of 1 in the X-Ray Structure of the Wlarg Aminotransferase From Campylobacter Jejuni in Complex with Tdp-QUI3N


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure of the Wlarg Aminotransferase From Campylobacter Jejuni in Complex with Tdp-QUI3N within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl406 b:11.6 occ:1.00 NE2 C:HIS298 3.2 9.3 1.0 CE1 C:TYR294 3.7 8.2 1.0 CD1 C:TYR294 3.9 7.6 1.0 CE1 C:HIS298 4.0 12.1 1.0 O C:HOH647 4.0 11.2 1.0 CD2 C:HIS298 4.3 9.6 1.0 O C:HOH818 4.8 12.5 1.0 CZ C:TYR294 4.9 7.2 1.0 O C:HOH901 4.9 13.8 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: ESSN 1469-896X
PubMed: 28028852
DOI: 10.1002/PRO.3109