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Zinc in PDB 2nqz: Trna-Guanine Transglycosylase (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine

Enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine, PDB code: 2nqz 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 / 1.46
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.900, 64.930, 71.180, 90.00, 96.36, 90.00
R / Rfree (%) 15 / 19.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine (pdb code 2nqz). 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 (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine, PDB code: 2nqz:

Zinc binding site 1 out of 1 in 2nqz

Go back to Zinc Binding Sites List in 2nqz
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine


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 (Tgt) Mutant in Complex with 7-Deaza-7- Aminomethyl-Guanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:16.9
occ:1.00
 ND1 A:HIS349 2.1 16.6 1.0
SG A:CYS318 2.3 18.2 1.0
SG A:CYS320 2.3 16.7 1.0
SG A:CYS323 2.3 17.1 1.0
CE1 A:HIS349 2.8 17.9 1.0
CB A:CYS318 3.2 18.6 1.0
CG A:HIS349 3.3 14.3 1.0
CB A:CYS323 3.4 17.6 1.0
CB A:CYS320 3.4 18.1 1.0
CB A:HIS349 3.7 15.0 1.0
N A:CYS323 3.9 16.5 1.0
NE2 A:HIS349 4.1 17.7 1.0
N A:CYS320 4.1 17.4 1.0
CA A:HIS349 4.1 15.2 1.0
CA A:CYS320 4.2 19.1 1.0
CA A:CYS323 4.2 16.7 1.0
CD2 A:HIS349 4.3 16.2 1.0
CA A:CYS318 4.5 18.2 1.0
O A:HIS349 4.6 16.6 1.0
O A:CYS320 4.6 18.4 1.0
C A:CYS320 4.6 18.3 1.0
C A:CYS318 4.7 18.7 1.0
C A:HIS349 4.8 14.4 1.0
CB A:VAL322 4.8 16.8 1.0
O A:CYS318 4.8 19.6 1.0
C A:VAL322 5.0 17.1 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 17 02:16:40 2024

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