Zinc in PDB 8wig: Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A

All present enzymatic activity of Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A:
6.1.1.3;

The structure of Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A, PDB code: 8wig was solved by H.Qiao, Z.Wang, J.Wang, P.Fang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	56.21 / 3.22
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	90.127, 108.179, 112.418, 90, 90, 90
R / Rfree (%)	20.8 / 22.2

The binding sites of Zinc atom in the Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A (pdb code 8wig). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A, PDB code: 8wig:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:58.0 occ:1.00 SG A:CYS334 2.3 60.1 1.0 NE2 A:HIS385 2.3 59.9 1.0 ND1 A:HIS511 2.3 59.8 1.0 CE1 A:HIS385 2.9 60.0 1.0 CG A:HIS511 3.2 59.6 1.0 CB A:HIS511 3.3 59.2 1.0 CE1 A:HIS511 3.3 60.5 1.0 CD2 A:HIS385 3.5 60.0 1.0 CB A:CYS334 3.7 60.9 1.0 ND1 A:HIS385 4.1 59.6 1.0 OH A:TYR462 4.1 63.4 0.8 CD2 A:HIS511 4.3 60.4 1.0 CA A:HIS511 4.4 58.4 1.0 OD2 A:ASP383 4.4 61.2 0.8 NE2 A:HIS511 4.4 60.6 1.0 CG A:HIS385 4.4 59.6 1.0 CA A:CYS334 4.4 61.4 1.0 N A:CYS334 4.5 62.2 1.0 OD1 A:ASP383 4.5 60.1 0.8 CG A:ASP383 4.6 60.3 0.8 SD A:MET332 4.9 73.6 0.8

Zinc binding site 2 out of 2 in the Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of E. Coli Thrs Catalytic Domain Mutant G463S/Q484A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:62.3 occ:0.84 SG B:CYS334 2.3 62.7 0.9 ND1 B:HIS511 2.3 64.8 0.9 NE2 B:HIS385 2.3 63.7 1.0 CE1 B:HIS385 2.9 63.3 1.0 CG B:HIS511 3.2 65.4 0.9 CE1 B:HIS511 3.3 65.1 0.9 CB B:HIS511 3.3 66.0 0.9 CD2 B:HIS385 3.4 64.0 1.0 OD2 B:ASP383 3.5 62.9 0.8 CB B:CYS334 3.8 63.0 0.9 ND1 B:HIS385 4.1 63.2 1.0 CD2 B:HIS511 4.4 65.8 0.9 CG B:HIS385 4.4 63.5 1.0 CA B:HIS511 4.4 65.7 0.9 NE2 B:HIS511 4.4 65.4 0.9 CA B:CYS334 4.4 62.8 0.9 N B:CYS334 4.5 63.0 0.9 CG B:ASP383 4.5 63.0 0.8 CE B:MET332 4.7 75.8 0.9 OH B:TYR462 4.8 66.9 0.8

H.Qiao, Z.Wang, H.Yang, M.Xia, G.Yang, F.Bai, J.Wang, P.Fang. Specific Glycine-Dependent Enzyme Motion Determines the Potency of Conformation Selective Inhibitors of Threonyl-Trna Synthetase. Commun Biol V. 7 867 2024.
ISSN: ESSN 2399-3642
PubMed: 39014102
DOI: 10.1038/S42003-024-06559-X