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Zinc in PDB 4hsh: Trna-Guanine Transglycosylase Y106F, V233G Mutant in Complex with Queuine

Enzymatic activity of Trna-Guanine Transglycosylase Y106F, V233G Mutant in Complex with Queuine

All present enzymatic activity of Trna-Guanine Transglycosylase Y106F, V233G Mutant in Complex with Queuine:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase Y106F, V233G Mutant in Complex with Queuine, PDB code: 4hsh was solved by I.Biela, 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) 20.89 / 1.56
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.554, 64.778, 70.479, 90.00, 95.95, 90.00
R / Rfree (%) 15.5 / 18.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase Y106F, V233G Mutant in Complex with Queuine (pdb code 4hsh). 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, V233G Mutant in Complex with Queuine, PDB code: 4hsh:

Zinc binding site 1 out of 1 in 4hsh

Go back to Zinc Binding Sites List in 4hsh
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase Y106F, V233G Mutant in Complex with Queuine


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, V233G Mutant in Complex with Queuine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:13.0
occ:1.00
ND1 A:HIS349 2.1 11.6 1.0
SG A:CYS320 2.3 12.2 1.0
SG A:CYS318 2.3 14.2 1.0
SG A:CYS323 2.3 12.1 1.0
CE1 A:HIS349 2.9 11.4 1.0
CG A:HIS349 3.3 9.6 1.0
CB A:CYS323 3.3 13.7 1.0
CB A:CYS318 3.3 13.6 1.0
CB A:CYS320 3.4 11.2 1.0
CB A:HIS349 3.8 11.0 1.0
N A:CYS323 3.9 12.7 1.0
N A:CYS320 4.1 14.2 1.0
CA A:HIS349 4.1 10.6 1.0
NE2 A:HIS349 4.1 12.0 1.0
CA A:CYS323 4.2 14.3 1.0
CA A:CYS320 4.2 13.2 1.0
CD2 A:HIS349 4.3 10.5 1.0
O A:HIS349 4.6 10.1 1.0
CA A:CYS318 4.6 15.6 1.0
C A:CYS320 4.7 14.8 1.0
O A:CYS320 4.7 15.1 1.0
C A:CYS318 4.7 16.3 1.0
C A:HIS349 4.8 11.5 1.0
CB A:VAL322 4.8 12.0 1.0
O A:CYS318 4.8 20.1 1.0
C A:VAL322 4.9 14.1 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: Sun Oct 27 00:16:48 2024

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