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Zinc in PDB 3bld: Trna Guanine Transglycosylase V233G Mutant PREQ1 Complex Structure

Enzymatic activity of Trna Guanine Transglycosylase V233G Mutant PREQ1 Complex Structure

All present enzymatic activity of Trna Guanine Transglycosylase V233G Mutant PREQ1 Complex Structure:
2.4.2.29;

Protein crystallography data

The structure of Trna Guanine Transglycosylase V233G Mutant PREQ1 Complex Structure, PDB code: 3bld 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 / 1.19
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.655, 64.878, 70.328, 90.00, 95.55, 90.00
R / Rfree (%) 15.1 / 18.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna Guanine Transglycosylase V233G Mutant PREQ1 Complex Structure (pdb code 3bld). 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 PREQ1 Complex Structure, PDB code: 3bld:

Zinc binding site 1 out of 1 in 3bld

Go back to Zinc Binding Sites List in 3bld
Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase V233G Mutant PREQ1 Complex 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 PREQ1 Complex Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn600

b:13.5
occ:1.00
ND1 A:HIS349 2.1 13.0 1.0
SG A:CYS323 2.3 14.1 1.0
SG A:CYS320 2.3 13.1 1.0
SG A:CYS318 2.3 15.2 1.0
CE1 A:HIS349 3.0 14.5 1.0
CB A:CYS323 3.2 14.0 1.0
CG A:HIS349 3.3 11.8 1.0
CB A:CYS318 3.3 16.2 1.0
CB A:CYS320 3.4 13.4 1.0
CB A:HIS349 3.8 12.6 1.0
N A:CYS323 3.9 13.5 1.0
CA A:HIS349 4.1 12.0 1.0
N A:CYS320 4.1 14.8 1.0
NE2 A:HIS349 4.2 13.8 1.0
CA A:CYS323 4.2 13.4 1.0
CA A:CYS320 4.2 14.0 1.0
CD2 A:HIS349 4.3 13.0 1.0
O A:HIS349 4.5 12.1 1.0
CA A:CYS318 4.6 17.1 1.0
C A:CYS320 4.7 13.8 1.0
O A:CYS320 4.7 14.7 1.0
C A:CYS318 4.7 16.3 1.0
C A:HIS349 4.8 11.4 1.0
CB A:VAL322 4.8 13.1 1.0
O A:CYS318 4.8 17.9 1.0
C A:VAL322 4.9 13.6 1.0

Reference:

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
Page generated: Thu Oct 24 11:32:53 2024

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