Zinc in PDB 4p3p: Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3

All present enzymatic activity of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3:
6.1.1.3;

The structure of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3, PDB code: 4p3p was solved by P.Fang, X.Yu, K.Chen, X.Chen, M.Guo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.80 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	94.534, 107.640, 109.623, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 21.9

The binding sites of Zinc atom in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3 (pdb code 4p3p). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3, PDB code: 4p3p:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:18.2 occ:1.00 NE2 A:HIS385 2.1 16.1 1.0 ND1 A:HIS511 2.2 14.5 1.0 O A:HOH934 2.3 19.2 1.0 SG A:CYS334 2.4 13.5 1.0 CE1 A:HIS511 3.0 14.7 1.0 CE1 A:HIS385 3.0 15.6 1.0 CB A:CYS334 3.1 13.7 1.0 CD2 A:HIS385 3.1 16.7 1.0 O A:HOH893 3.2 16.8 1.0 CG A:HIS511 3.4 15.1 1.0 CB A:HIS511 3.9 15.0 1.0 OD2 A:ASP383 4.0 19.1 1.0 CA A:CYS334 4.0 13.2 1.0 OD1 A:ASP383 4.1 19.6 1.0 C9 A:2CR702 4.1 17.1 1.0 N A:CYS334 4.1 12.8 1.0 ND1 A:HIS385 4.2 15.8 1.0 NE2 A:HIS511 4.2 15.3 1.0 O A:HOH888 4.2 14.2 1.0 CG A:HIS385 4.2 16.4 1.0 CD2 A:HIS511 4.4 15.5 1.0 CG A:ASP383 4.5 19.3 1.0 CA A:HIS511 4.7 15.1 1.0 C8 A:2CR702 4.8 17.5 1.0 C5 A:2CR702 4.9 16.9 1.0 C7 A:2CR702 5.0 17.5 1.0

Zinc binding site 2 out of 2 in the Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis For Full-Spectrum Inhibition of Threonyl-Trna Synthetase By Borrelidin 3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:21.4 occ:1.00 ND1 B:HIS511 2.1 12.3 1.0 NE2 B:HIS385 2.1 15.1 1.0 SG B:CYS334 2.2 13.6 1.0 O B:HOH920 2.3 28.4 1.0 CE1 B:HIS511 2.7 12.5 1.0 CB B:CYS334 2.8 13.7 1.0 CD2 B:HIS385 3.1 15.3 1.0 CE1 B:HIS385 3.2 14.7 1.0 O B:HOH900 3.3 29.1 1.0 CG B:HIS511 3.3 12.8 1.0 CA B:CYS334 3.8 13.2 1.0 CB B:HIS511 3.9 12.7 1.0 NE2 B:HIS511 3.9 13.0 1.0 OD2 B:ASP383 4.0 19.8 1.0 N B:CYS334 4.1 12.9 1.0 O B:HOH865 4.1 21.8 1.0 C9 B:2CR702 4.1 16.7 1.0 OD1 B:ASP383 4.1 20.1 1.0 CG B:HIS385 4.2 15.0 1.0 CD2 B:HIS511 4.2 13.1 1.0 ND1 B:HIS385 4.3 14.5 1.0 CG B:ASP383 4.5 19.9 1.0 CA B:HIS511 4.7 12.7 1.0 C8 B:2CR702 4.8 17.1 1.0 C7 B:2CR702 4.9 17.1 1.0 C10 B:2CR702 5.0 17.0 1.0

P.Fang, X.Yu, S.Jeong, A.Mirando, K.Chen, X.Chen, S.Kim, C.S.Francklyn, M.Guo. Structural Basis For Full-Spectrum Inhibition of Translational and Nontranslational Functions on A Human Trna Synthetase To Be Published.