Zinc in PDB 3bl3: Trna Guanine Transglycosylase V233G Mutant Apo Structure

All present enzymatic activity of Trna Guanine Transglycosylase V233G Mutant Apo Structure:
2.4.2.29;

The structure of Trna Guanine Transglycosylase V233G Mutant Apo Structure, PDB code: 3bl3 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)	50.00 / 2.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.686, 64.774, 70.400, 90.00, 95.94, 90.00
R / Rfree (%)	18.7 / 22.7

The binding sites of Zinc atom in the Trna Guanine Transglycosylase V233G Mutant Apo Structure (pdb code 3bl3). 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 V233G Mutant Apo Structure, PDB code: 3bl3:

Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase V233G Mutant 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 V233G Mutant Apo Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:20.6 occ:1.00 ND1 A:HIS349 2.3 9.8 1.0 SG A:CYS318 2.4 16.4 1.0 SG A:CYS320 2.4 18.4 1.0 SG A:CYS323 2.4 18.1 1.0 CE1 A:HIS349 3.0 11.7 1.0 CB A:CYS318 3.1 18.1 1.0 CB A:CYS323 3.3 16.2 1.0 CG A:HIS349 3.4 12.5 1.0 CB A:CYS320 3.4 15.3 1.0 CB A:HIS349 3.9 12.4 1.0 N A:CYS323 3.9 17.3 1.0 CA A:HIS349 4.1 13.4 1.0 N A:CYS320 4.2 16.7 1.0 NE2 A:HIS349 4.2 11.1 1.0 CA A:CYS323 4.2 17.9 1.0 CA A:CYS320 4.3 16.1 1.0 CD2 A:HIS349 4.4 11.1 1.0 CA A:CYS318 4.5 20.1 1.0 O A:HIS349 4.6 13.5 1.0 O A:CYS320 4.7 14.0 1.0 CB A:VAL322 4.7 15.4 1.0 C A:CYS318 4.7 20.0 1.0 C A:HIS349 4.7 13.7 1.0 C A:CYS320 4.7 15.2 1.0 C A:VAL322 4.9 16.8 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