Chlorine in PDB 4hws: Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor

All present enzymatic activity of Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor:
6.1.1.3;

The structure of Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor, PDB code: 4hws was solved by M.T.Hilgers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.35 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.181, 110.327, 114.866, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 21.7

The structure of Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor (pdb code 4hws). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor, PDB code: 4hws:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor


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 E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl702 b:20.1 occ:1.00 CL2 A:1B3702 0.0 20.1 1.0 C25 A:1B3702 1.8 21.2 1.0 N24 A:1B3702 2.6 20.6 1.0 N26 A:1B3702 2.7 19.6 1.0 O A:LEU373 2.8 19.0 1.0 O A:MET374 3.3 22.2 1.0 OG A:SER517 3.5 18.0 1.0 C A:MET374 3.5 22.1 1.0 CG2 A:VAL376 3.6 18.8 1.0 N A:ARG520 3.7 17.5 1.0 CB A:GLU519 3.8 17.4 1.0 C A:LEU373 3.8 19.5 1.0 CB A:ARG520 3.8 17.7 1.0 N A:VAL376 3.9 19.8 1.0 C22 A:1B3702 3.9 20.5 1.0 N A:ARG375 3.9 21.3 1.0 C27 A:1B3702 3.9 19.9 1.0 CA A:MET374 4.0 22.4 1.0 CA A:ARG520 4.1 17.6 1.0 CG1 A:VAL376 4.1 18.9 1.0 CA A:ARG375 4.1 21.4 1.0 N A:MET374 4.3 21.2 1.0 CB A:VAL376 4.3 19.1 1.0 CB A:PHE379 4.4 17.4 1.0 C A:GLU519 4.4 17.4 1.0 C21 A:1B3702 4.4 19.7 1.0 C A:ARG375 4.5 20.8 1.0 NE A:ARG520 4.5 18.2 1.0 CB A:SER517 4.5 17.3 1.0 CA A:GLU519 4.7 17.3 1.0 CA A:VAL376 4.7 19.4 1.0 CG A:GLU519 4.9 17.4 1.0 NH2 A:ARG520 4.9 19.0 1.0 CG A:ARG520 4.9 17.9 1.0 CA A:LEU373 5.0 18.9 1.0 N28 A:1B3702 5.0 21.1 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of E. Coli Threonyl-Trna Synthetase Bound to A Novel Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl702 b:20.1 occ:1.00 CL2 B:1B3702 0.0 20.1 1.0 C25 B:1B3702 1.7 20.1 1.0 N26 B:1B3702 2.6 20.8 1.0 N24 B:1B3702 2.7 20.6 1.0 O B:LEU373 2.8 20.0 1.0 O B:MET374 3.3 21.2 1.0 C B:MET374 3.5 21.4 1.0 CG2 B:VAL376 3.5 19.0 1.0 OG B:SER517 3.5 18.2 1.0 N B:ARG520 3.7 18.2 1.0 CB B:GLU519 3.8 18.3 1.0 C B:LEU373 3.8 20.2 1.0 N B:VAL376 3.8 20.1 1.0 N B:ARG375 3.8 21.2 1.0 CB B:ARG520 3.9 18.7 1.0 C22 B:1B3702 3.9 21.1 1.0 C27 B:1B3702 3.9 20.7 1.0 CG1 B:VAL376 4.0 18.7 1.0 CA B:ARG520 4.0 18.7 1.0 CA B:ARG375 4.0 21.7 1.0 CA B:MET374 4.1 22.0 1.0 CB B:VAL376 4.3 18.9 1.0 C B:GLU519 4.4 18.1 1.0 N B:MET374 4.4 21.0 1.0 C B:ARG375 4.4 21.6 1.0 CB B:PHE379 4.4 18.1 1.0 C21 B:1B3702 4.5 20.1 1.0 NE B:ARG520 4.5 19.5 1.0 CB B:SER517 4.6 18.4 1.0 CA B:VAL376 4.7 19.8 1.0 CA B:GLU519 4.7 18.4 1.0 CG B:GLU519 4.8 18.9 1.0 CG B:ARG520 4.9 19.2 1.0 CA B:LEU373 4.9 20.2 1.0 NH2 B:ARG520 4.9 20.3 1.0 N28 B:1B3702 5.0 19.4 1.0 CG B:PHE379 5.0 18.5 1.0

M.Teng, M.T.Hilgers, M.L.Cunningham, A.Borchardt, J.B.Locke, S.Abraham, G.Haley, B.P.Kwan, C.Hall, G.W.Hough, K.J.Shaw, J.Finn. Identification of Bacteria-Selective Threonyl-Trna Synthetase Substrate Inhibitors By Structure-Based Design. J.Med.Chem. V. 56 1748 2013.
ISSN: ISSN 0022-2623
PubMed: 23362938
DOI: 10.1021/JM301756M