Chlorine in PDB 4q5r: Crystal Structure of Glutathione S-Transferase Bla G 5

All present enzymatic activity of Crystal Structure of Glutathione S-Transferase Bla G 5:
2.5.1.18;

The structure of Crystal Structure of Glutathione S-Transferase Bla G 5, PDB code: 4q5r was solved by L.C.Pedersen, G.A.Mueller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.62 / 2.25
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	72.063, 102.379, 165.765, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 24.5

The binding sites of Chlorine atom in the Crystal Structure of Glutathione S-Transferase Bla G 5 (pdb code 4q5r). 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 Crystal Structure of Glutathione S-Transferase Bla G 5, PDB code: 4q5r:

Chlorine binding site 1 out of 1 in the Crystal Structure of Glutathione S-Transferase Bla G 5


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Glutathione S-Transferase Bla G 5 within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl303 b:40.4 occ:1.00 N D:CYS10 3.0 36.7 1.0 NH2 D:ARG20 3.0 41.9 1.0 NH1 D:ARG20 3.2 36.0 1.0 N D:GLY16 3.3 22.2 1.0 O D:CYS10 3.5 45.3 1.0 CA D:GLY16 3.5 22.7 1.0 CZ D:ARG20 3.5 35.9 1.0 O D:HOH515 3.6 43.6 1.0 CA D:ALA14 3.6 41.6 1.0 CB D:TYR9 3.7 38.6 1.0 CB D:CYS10 3.8 37.8 1.0 CA D:CYS10 3.8 40.9 1.0 C D:ALA14 3.8 42.7 1.0 CA D:TYR9 3.8 33.8 1.0 C D:TYR9 3.9 37.5 1.0 N D:LEU15 4.0 36.9 1.0 C D:CYS10 4.0 46.4 1.0 C D:GLY16 4.1 23.9 1.0 N D:GLU17 4.2 23.6 1.0 O D:ALA14 4.4 47.0 1.0 CB D:ALA14 4.4 36.7 1.0 C D:LEU15 4.5 25.6 1.0 N D:ALA14 4.5 43.6 1.0 CG D:TYR9 4.6 40.9 1.0 CD1 D:TYR9 4.6 39.1 1.0 NE D:ARG20 4.8 29.9 1.0 O D:HOH518 4.9 45.7 1.0 CA D:LEU15 4.9 31.0 1.0 SG D:CYS10 4.9 60.3 1.0 O D:GLY16 5.0 25.9 1.0

L.C.Pedersen, G.A.Mueller. Crystal Structure of Glutathione S-Transferase Bla G 5 To Be Published.