Zinc in PDB 4q8m: Trna-Guanine Transglycosylase (Tgt) Mutant V262T Apo Structure

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Mutant V262T Apo Structure:
2.4.2.29;

The structure of Trna-Guanine Transglycosylase (Tgt) Mutant V262T Apo Structure, PDB code: 4q8m was solved by M.Neeb, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	17.52 / 1.24
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.412, 64.776, 70.289, 90.00, 95.58, 90.00
R / Rfree (%)	14.2 / 16

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) Mutant V262T Apo Structure (pdb code 4q8m). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Trna-Guanine Transglycosylase (Tgt) Mutant V262T Apo Structure, PDB code: 4q8m:

Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) Mutant V262T Apo Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Trna-Guanine Transglycosylase (Tgt) Mutant V262T Apo Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:11.4 occ:1.00 ND1 A:HIS349 2.1 11.3 1.0 SG A:CYS323 2.3 11.7 1.0 SG A:CYS320 2.3 11.4 1.0 SG A:CYS318 2.3 13.1 1.0 CE1 A:HIS349 2.9 11.1 1.0 CG A:HIS349 3.2 10.7 1.0 CB A:CYS318 3.3 13.6 1.0 CB A:CYS323 3.3 11.9 1.0 CB A:CYS320 3.4 11.8 1.0 CB A:HIS349 3.7 10.8 1.0 N A:CYS323 3.9 11.5 1.0 CA A:HIS349 4.1 9.8 1.0 NE2 A:HIS349 4.1 11.4 1.0 N A:CYS320 4.1 13.4 1.0 CA A:CYS323 4.2 11.7 1.0 CA A:CYS320 4.2 12.6 1.0 CD2 A:HIS349 4.3 10.9 1.0 O A:HIS349 4.5 10.0 1.0 CA A:CYS318 4.6 14.6 1.0 O A:CYS320 4.7 12.8 1.0 C A:CYS320 4.7 12.2 1.0 C A:CYS318 4.7 15.7 1.0 C A:HIS349 4.8 9.7 1.0 CB A:VAL322 4.8 11.2 1.0 O A:CYS318 4.8 15.7 1.0 C A:VAL322 4.9 10.8 1.0

M.Neeb, A.Heine, G.Klebe. Creating A Resistance Model For Tgt: the Effect of Mutations on Flexible Lin-Benzoguanine Substituents To Be Published.