Zinc in PDB 6l2p: Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form

All present enzymatic activity of Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form:
6.1.1.3;

The structure of Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form, PDB code: 6l2p was solved by J.Guo, B.Chen, H.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.988, 101.859, 106.047, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 26.1

The binding sites of Zinc atom in the Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form (pdb code 6l2p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form, PDB code: 6l2p:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:35.5 occ:1.00 SG A:CYS334 2.2 36.6 1.0 NE2 A:HIS385 2.2 37.8 1.0 ND1 A:HIS511 2.4 40.9 1.0 CE1 A:HIS385 2.9 37.0 1.0 CE1 A:HIS511 3.1 40.9 1.0 CG A:HIS511 3.3 39.0 1.0 CB A:CYS334 3.3 36.0 1.0 CD2 A:HIS385 3.4 38.1 1.0 CB A:HIS511 3.7 37.7 1.0 OD1 A:ASP383 3.8 55.8 1.0 O A:HOH809 4.0 27.8 1.0 OD2 A:ASP383 4.0 54.0 1.0 ND1 A:HIS385 4.1 36.7 1.0 NE2 A:HIS511 4.1 40.4 1.0 CA A:CYS334 4.1 35.9 1.0 CD2 A:HIS511 4.2 39.3 1.0 CG A:ASP383 4.3 52.0 1.0 N A:CYS334 4.3 36.2 1.0 CG A:HIS385 4.4 36.8 1.0 CA A:HIS511 4.5 36.7 1.0 O A:HOH866 4.7 55.5 1.0

Zinc binding site 2 out of 2 in the Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Threonyl-Trna Synthetase From Salmonella Enterica in the Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:46.1 occ:1.00 SG B:CYS334 2.3 49.4 1.0 NE2 B:HIS385 2.4 47.7 1.0 ND1 B:HIS511 2.6 50.0 1.0 CE1 B:HIS385 2.9 46.3 1.0 CG B:HIS511 3.3 48.9 1.0 CE1 B:HIS511 3.3 50.8 1.0 CB B:CYS334 3.5 49.6 1.0 CD2 B:HIS385 3.5 46.9 1.0 CB B:HIS511 3.7 47.9 1.0 OD2 B:ASP383 3.8 51.0 1.0 OD1 B:ASP383 3.9 49.6 1.0 ND1 B:HIS385 4.1 45.7 1.0 CA B:CYS334 4.2 48.6 1.0 CG B:ASP383 4.3 48.9 1.0 NE2 B:HIS511 4.3 50.2 1.0 CD2 B:HIS511 4.3 49.6 1.0 N B:CYS334 4.4 48.0 1.0 CG B:HIS385 4.4 46.0 1.0 CA B:HIS511 4.6 47.2 1.0

J.Guo, B.Chen, Y.Yu, B.Cheng, Y.Cheng, Y.Ju, Q.Gu, J.Xu, H.Zhou. Discovery of Novel Trna-Amino Acid Dual-Site Inhibitors Against Threonyl-Trna Synthetase By Fragment-Based Target Hopping. Eur.J.Med.Chem. V. 187 11941 2019.
ISSN: ISSN 0223-5234
PubMed: 31821989
DOI: 10.1016/J.EJMECH.2019.111941