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Zinc in PDB 2z1x: Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ1

Enzymatic activity of Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ1

All present enzymatic activity of Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ1:
2.4.2.29;

Protein crystallography data

The structure of Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ1, PDB code: 2z1x was solved by N.Tidten, B.Stengl, A.Heine, G.A.Garcia, G.Klebe, K.Reuter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.10 / 1.63
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.138, 64.139, 69.856, 90.00, 92.88, 90.00
R / Rfree (%) 15.3 / 21.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ1 (pdb code 2z1x). 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 E235Q Mutant in Complex with PREQ1, PDB code: 2z1x:

Zinc binding site 1 out of 1 in 2z1x

Go back to Zinc Binding Sites List in 2z1x
Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ1


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 E235Q Mutant in Complex with PREQ1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:16.5
occ:1.00
ND1 A:HIS349 2.2 18.4 1.0
SG A:CYS323 2.3 17.5 1.0
SG A:CYS320 2.3 19.1 1.0
SG A:CYS318 2.3 20.2 1.0
CE1 A:HIS349 3.0 17.6 1.0
CB A:CYS323 3.2 18.7 1.0
CB A:CYS318 3.2 19.6 1.0
CG A:HIS349 3.3 15.9 1.0
CB A:CYS320 3.4 18.6 1.0
CB A:HIS349 3.7 14.8 1.0
N A:CYS323 3.9 15.8 1.0
CA A:HIS349 4.1 14.3 1.0
N A:CYS320 4.1 19.4 1.0
CA A:CYS323 4.1 19.7 1.0
NE2 A:HIS349 4.2 17.4 1.0
CA A:CYS320 4.2 19.1 1.0
CD2 A:HIS349 4.3 14.2 1.0
O A:HIS349 4.5 13.7 1.0
CA A:CYS318 4.5 19.0 1.0
O A:CYS320 4.6 18.4 1.0
C A:CYS320 4.6 17.7 1.0
C A:CYS318 4.7 21.9 1.0
CB A:VAL322 4.7 15.7 1.0
C A:HIS349 4.7 12.5 1.0
O A:CYS318 4.9 23.0 1.0
C A:VAL322 4.9 16.7 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: Thu Oct 24 10:33:01 2024

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