Chlorine in PDB 2ja2: Mycobacterium Tuberculosis Glutamyl-Trna Synthetase

All present enzymatic activity of Mycobacterium Tuberculosis Glutamyl-Trna Synthetase:
6.1.1.17;

The structure of Mycobacterium Tuberculosis Glutamyl-Trna Synthetase, PDB code: 2ja2 was solved by G.P.Bourenkov, N.Strizhov, L.A.Shkolnaya, M.Bruning, H.D.Bartunik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.52 / 1.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.130, 61.483, 169.547, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 25.1

The binding sites of Chlorine atom in the Mycobacterium Tuberculosis Glutamyl-Trna Synthetase (pdb code 2ja2). 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 Mycobacterium Tuberculosis Glutamyl-Trna Synthetase, PDB code: 2ja2:

Chlorine binding site 1 out of 1 in the Mycobacterium Tuberculosis Glutamyl-Trna Synthetase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mycobacterium Tuberculosis Glutamyl-Trna Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1487 b:26.8 occ:1.00 O A:HOH2229 3.1 31.3 1.0 N A:VAL250 3.2 19.3 1.0 O A:HOH2017 3.3 32.1 1.0 O A:HOH2227 3.3 25.4 1.0 NH2 A:ARG25 3.5 17.1 1.0 CG2 A:VAL250 3.9 16.0 1.0 CA A:THR249 3.9 17.1 1.0 CA A:GLY22 3.9 18.5 1.0 CB A:VAL250 4.0 17.1 1.0 CE A:LYS257 4.0 33.5 1.0 C A:THR249 4.0 18.8 1.0 O A:HOH2040 4.1 34.5 1.0 CA A:VAL250 4.1 16.0 1.0 CG2 A:THR249 4.1 24.1 1.0 C A:GLY22 4.4 16.1 1.0 O A:GLY22 4.4 17.6 1.0 O A:PRO248 4.4 18.1 1.0 NZ A:LYS257 4.5 32.5 1.0 CB A:THR249 4.5 18.0 1.0 CZ A:ARG25 4.6 15.7 1.0 O A:VAL250 4.7 20.0 1.0 OG1 A:THR249 4.9 19.9 1.0 C A:VAL250 4.9 19.0 1.0 N A:THR249 4.9 18.4 1.0

G.P.Bourenkov, M.Bruning, N.Strizhov, L.A.Shkolnaya, H.D.Bartunik. Structural Basis For Discriminating or Non- Discriminating Functioning of Glutamyl-Trna Synthetases To Be Published.