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Zinc in PDB 2qii: Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0

Enzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0

All present enzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0:
2.4.2.29;

Protein crystallography data

The structure of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0, PDB code: 2qii was solved by N.Tidten, R.Brenk, 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) 20.00 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.622, 65.535, 70.325, 90.00, 96.47, 90.00
R / Rfree (%) 16.6 / 21.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0 (pdb code 2qii). 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 Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0, PDB code: 2qii:

Zinc binding site 1 out of 1 in 2qii

Go back to Zinc Binding Sites List in 2qii
Zinc binding site 1 out of 1 in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:19.4
occ:1.00
 ND1 A:HIS349 2.1 17.9 1.0
SG A:CYS320 2.3 19.5 1.0
SG A:CYS318 2.3 21.7 1.0
SG A:CYS323 2.4 19.2 1.0
CE1 A:HIS349 2.9 16.8 1.0
CB A:CYS318 3.3 22.1 1.0
CB A:CYS323 3.3 18.8 1.0
CG A:HIS349 3.3 16.8 1.0
CB A:CYS320 3.3 19.2 1.0
CB A:HIS349 3.8 17.6 1.0
N A:CYS323 3.9 21.7 1.0
N A:CYS320 4.0 19.7 1.0
NE2 A:HIS349 4.1 15.6 1.0
CA A:HIS349 4.1 19.3 1.0
CA A:CYS320 4.2 19.6 1.0
CA A:CYS323 4.2 16.9 1.0
CD2 A:HIS349 4.3 15.8 1.0
O A:HIS349 4.5 15.2 1.0
CA A:CYS318 4.6 19.6 1.0
C A:CYS318 4.6 19.2 1.0
C A:CYS320 4.6 19.6 1.0
O A:CYS320 4.7 16.5 1.0
O A:CYS318 4.7 23.2 1.0
CB A:VAL322 4.8 17.4 1.0
C A:HIS349 4.8 18.0 1.0
C A:VAL322 4.9 20.2 1.0

Reference:

N.Tidten, B.Stengl, A.Heine, G.A.Garcia, G.Klebe, K.Reuter. Glutamate Versus Glutamine Exchange Swaps Substrate Selectivity in Trna-Guanine Transglycosylase: Insight Into the Regulation of Substrate Selectivity By Kinetic and Crystallographic Studies. J.Mol.Biol. V. 374 764 2007.
ISSN: ISSN 0022-2836
PubMed: 17949745
DOI: 10.1016/J.JMB.2007.09.062
Page generated: Wed Aug 20 05:24:26 2025

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