Chlorine in PDB 5jzs: Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid

All present enzymatic activity of Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid:
3.7.1.8;

The structure of Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid, PDB code: 5jzs was solved by A.Ryan, E.Polycarpou, N.Lack, D.Evangelopoulos, C.Sieg, A.Halman, S.Bhakta, A.Sinclair, O.Eleftheriadou, T.D.Mchugh, S.Keany, E.D.Lowe, R.Ballet, A.Abuhammad, A.Ciulli, E.Sim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	97.57 / 2.27
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	81.920, 82.270, 195.130, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 23.5

The binding sites of Chlorine atom in the Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid (pdb code 5jzs). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid, PDB code: 5jzs:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1000 b:80.4 occ:0.90 CL1 B:FGZ1000 0.0 80.4 0.9 C06 B:FGZ1000 1.8 62.9 0.9 C05 B:FGZ1000 2.7 49.1 0.9 C08 B:FGZ1000 2.7 57.6 0.9 O09 B:FGZ1000 3.0 57.1 0.9 O B:HOH1153 3.7 42.6 1.0 C04 B:FGZ1000 4.0 51.3 0.9 C10 B:FGZ1000 4.0 54.9 0.9 CD1 B:LEU115 4.2 39.7 1.0 O B:HOH1152 4.5 55.9 1.0 C12 B:FGZ1000 4.5 50.0 0.9 CZ B:PHE212 4.7 66.0 1.0 CB B:LEU115 4.8 35.1 1.0 CG B:LEU115 4.9 41.5 1.0 CD2 B:LEU115 4.9 40.5 1.0 CD2 B:LEU158 5.0 50.8 1.0

Chlorine binding site 2 out of 2 in the Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Hsad Bound to 3,5-Dichloro-4-Hydroxybenzoic Acid within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1000 b:60.8 occ:0.90 CL2 B:FGZ1000 0.0 60.8 0.9 C10 B:FGZ1000 1.8 54.9 0.9 C12 B:FGZ1000 2.7 50.0 0.9 C08 B:FGZ1000 2.8 57.6 0.9 O09 B:FGZ1000 3.1 57.1 0.9 CD2 B:LEU158 3.2 50.8 1.0 O B:GLY154 3.5 31.1 1.0 CA B:VAL155 3.5 32.6 1.0 CG1 B:VAL243 3.6 35.2 1.0 C B:GLY154 3.7 34.0 1.0 N B:VAL155 3.7 36.0 1.0 CB B:LEU158 3.7 37.6 1.0 CE1 B:PHE173 3.8 48.5 1.0 CG2 B:VAL155 3.8 35.8 1.0 C04 B:FGZ1000 4.0 51.3 0.9 C06 B:FGZ1000 4.1 62.9 0.9 CG B:LEU158 4.1 47.2 1.0 CB B:VAL155 4.3 30.2 1.0 CZ B:PHE173 4.4 48.8 1.0 C05 B:FGZ1000 4.5 49.1 0.9 C B:VAL155 4.6 28.5 1.0 CG2 B:VAL243 4.6 27.4 1.0 CB B:VAL243 4.7 31.6 1.0 O B:VAL155 4.7 32.9 1.0 CA B:GLY154 4.7 35.6 1.0 CD1 B:PHE173 4.8 42.7 1.0 CG1 B:VAL155 4.9 25.1 1.0

A.Ryan, E.Polycarpou, N.A.Lack, D.Evangelopoulos, C.Sieg, A.Halman, S.Bhakta, O.Eleftheriadou, T.D.Mchugh, S.Keany, E.D.Lowe, R.Ballet, A.Abuhammad, W.R.Jacobs, A.Ciulli, E.Sim. Investigation of the Mycobacterial Enzyme Hsad As A Potential Novel Target For Anti-Tubercular Agents Using A Fragment-Based Drug Design Approach. Br. J. Pharmacol. V. 174 2209 2017.
ISSN: ISSN 1476-5381
PubMed: 28380256
DOI: 10.1111/BPH.13810