Zinc in PDB 3bll: Tgt Mutant in Complex with Boc-PREQ1

All present enzymatic activity of Tgt Mutant in Complex with Boc-PREQ1:
2.4.2.29;

The structure of Tgt Mutant in Complex with Boc-PREQ1, PDB code: 3bll 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)	8.00 / 1.26
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	89.949, 64.849, 70.471, 90.00, 95.56, 90.00
R / Rfree (%)	14.9 / 18.2

The binding sites of Zinc atom in the Tgt Mutant in Complex with Boc-PREQ1 (pdb code 3bll). 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 Tgt Mutant in Complex with Boc-PREQ1, PDB code: 3bll:

Zinc binding site 1 out of 1 in the Tgt Mutant in Complex with Boc-PREQ1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Tgt Mutant in Complex with Boc-PREQ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn600 b:15.9 occ:1.00 ND1 A:HIS349 2.2 15.9 1.0 SG A:CYS318 2.3 18.1 1.0 SG A:CYS320 2.3 16.0 1.0 SG A:CYS323 2.3 16.3 1.0 CE1 A:HIS349 3.0 16.8 1.0 CB A:CYS323 3.3 15.6 1.0 CB A:CYS318 3.3 19.9 1.0 CG A:HIS349 3.3 13.3 1.0 CB A:CYS320 3.4 17.2 1.0 CB A:HIS349 3.8 14.6 1.0 N A:CYS323 3.9 16.7 1.0 CA A:HIS349 4.1 12.2 1.0 N A:CYS320 4.2 18.5 1.0 NE2 A:HIS349 4.2 14.1 1.0 CA A:CYS323 4.2 17.6 1.0 CA A:CYS320 4.3 17.6 1.0 CD2 A:HIS349 4.4 14.4 1.0 O A:HIS349 4.6 13.6 1.0 CA A:CYS318 4.6 19.3 1.0 C A:CYS320 4.7 15.1 1.0 O A:CYS320 4.7 17.6 1.0 C A:CYS318 4.7 19.9 1.0 CB A:VAL322 4.8 14.8 1.0 C A:HIS349 4.8 14.0 1.0 O A:CYS318 4.8 21.5 1.0 C A:VAL322 5.0 16.7 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