Zinc in PDB 2nso: Trna-Gunanine-Transglycosylase (Tgt) Mutant Y106F, C158V, A232S, V233G- Apo-Structure

All present enzymatic activity of Trna-Gunanine-Transglycosylase (Tgt) Mutant Y106F, C158V, A232S, V233G- Apo-Structure:
2.4.2.29;

The structure of Trna-Gunanine-Transglycosylase (Tgt) Mutant Y106F, C158V, A232S, V233G- Apo-Structure, PDB code: 2nso was solved by N.Tidten, A.Heine, K.Reuter, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.42 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.730, 64.830, 70.810, 90.00, 96.31, 90.00
R / Rfree (%)	16.2 / 22.1

The binding sites of Zinc atom in the Trna-Gunanine-Transglycosylase (Tgt) Mutant Y106F, C158V, A232S, V233G- Apo-Structure (pdb code 2nso). 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-Gunanine-Transglycosylase (Tgt) Mutant Y106F, C158V, A232S, V233G- Apo-Structure, PDB code: 2nso:

Zinc binding site 1 out of 1 in the Trna-Gunanine-Transglycosylase (Tgt) Mutant Y106F, C158V, A232S, V233G- 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-Gunanine-Transglycosylase (Tgt) Mutant Y106F, C158V, A232S, V233G- Apo-Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:19.8 occ:1.00 ND1 A:HIS349 2.1 19.0 1.0 SG A:CYS320 2.3 20.1 1.0 SG A:CYS318 2.3 20.8 1.0 SG A:CYS323 2.3 21.0 1.0 CE1 A:HIS349 2.9 18.9 1.0 CB A:CYS318 3.2 21.7 1.0 CB A:CYS323 3.2 18.1 1.0 CB A:CYS320 3.3 21.3 1.0 CG A:HIS349 3.3 18.8 1.0 CB A:HIS349 3.8 18.5 1.0 N A:CYS323 3.9 19.4 1.0 NE2 A:HIS349 4.1 18.4 1.0 N A:CYS320 4.1 20.6 1.0 CA A:HIS349 4.1 18.1 1.0 CA A:CYS323 4.2 19.6 1.0 CA A:CYS320 4.2 19.5 1.0 CD2 A:HIS349 4.3 19.7 1.0 O A:HIS349 4.5 17.3 1.0 CA A:CYS318 4.5 22.0 1.0 O A:CYS320 4.6 18.5 1.0 C A:CYS320 4.6 19.2 1.0 C A:CYS318 4.6 22.1 1.0 C A:HIS349 4.8 17.3 1.0 O A:CYS318 4.8 24.9 1.0 CB A:VAL322 4.8 15.7 1.0 C A:VAL322 4.9 18.6 1.0

I.Biela, N.Tidten-Luksch, F.Immekus, S.Glinca, T.X.Nguyen, H.D.Gerber, A.Heine, G.Klebe, K.Reuter. Investigation of Specificity Determinants in Bacterial Trna-Guanine Transglycosylase Reveals Queuine, the Substrate of Its Eucaryotic Counterpart, As Inhibitor. Plos One V. 8 64240 2013.
ISSN: ESSN 1932-6203
PubMed: 23704982
DOI: 10.1371/JOURNAL.PONE.0064240