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Zinc in PDB 4gd0: Trna-Guanine Transglycosylase Y106F, C158V Mutant

Enzymatic activity of Trna-Guanine Transglycosylase Y106F, C158V Mutant

All present enzymatic activity of Trna-Guanine Transglycosylase Y106F, C158V Mutant:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase Y106F, C158V Mutant, PDB code: 4gd0 was solved by I.Schmidt, N.Tidten-Luksch, 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) 16.27 / 1.29
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.428, 64.986, 70.203, 90.00, 96.10, 90.00
R / Rfree (%) 16.3 / 18.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase Y106F, C158V Mutant (pdb code 4gd0). 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 Y106F, C158V Mutant, PDB code: 4gd0:

Zinc binding site 1 out of 1 in 4gd0

Go back to Zinc Binding Sites List in 4gd0
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase Y106F, C158V Mutant


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 Y106F, C158V Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:63.1
occ:1.00
O A:HOH887 2.7 40.4 1.0
O A:HOH524 2.9 12.2 1.0
O A:SER316 3.1 15.3 1.0
O A:HOH591 3.6 18.9 1.0
O A:GLU317 3.7 13.9 1.0
C A:GLU317 3.8 11.8 1.0
CA A:GLU317 3.8 12.5 1.0
C A:SER316 3.9 14.2 1.0
O A:HOH833 4.1 31.3 1.0
O A:CYS318 4.1 10.9 1.0
N A:GLU317 4.3 13.1 1.0
O A:HOH777 4.4 34.6 1.0
N A:CYS318 4.6 10.6 1.0
O A:HOH971 4.6 42.5 1.0
C A:CYS318 4.8 9.8 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: Sat Oct 26 23:14:30 2024

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