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Zinc in PDB 2pwv: Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ0

Enzymatic activity of Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ0

All present enzymatic activity of Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ0:
2.4.2.29;

Protein crystallography data

The structure of Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ0, PDB code: 2pwv was solved by N.Tidten, B.Stengl, 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) 10.00 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.757, 65.175, 70.455, 90.00, 96.12, 90.00
R / Rfree (%) 20.1 / 24.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ0 (pdb code 2pwv). 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 PREQ0, PDB code: 2pwv:

Zinc binding site 1 out of 1 in 2pwv

Go back to Zinc Binding Sites List in 2pwv
Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase E235Q Mutant in Complex with PREQ0


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 PREQ0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:19.0
occ:1.00
ND1 A:HIS349 2.1 12.6 1.0
SG A:CYS323 2.3 18.1 1.0
SG A:CYS318 2.3 20.1 1.0
SG A:CYS320 2.4 18.5 1.0
CE1 A:HIS349 2.8 21.1 1.0
CB A:CYS318 3.0 22.2 1.0
CB A:CYS323 3.3 18.8 1.0
CG A:HIS349 3.4 10.5 1.0
CB A:CYS320 3.4 19.9 1.0
N A:CYS323 3.8 18.3 1.0
CB A:HIS349 3.9 11.8 1.0
NE2 A:HIS349 4.0 14.4 1.0
N A:CYS320 4.1 18.3 1.0
CA A:CYS323 4.1 22.1 1.0
CA A:HIS349 4.2 18.0 1.0
CA A:CYS320 4.2 23.0 1.0
CD2 A:HIS349 4.3 18.4 1.0
CA A:CYS318 4.4 25.0 1.0
C A:CYS318 4.6 23.7 1.0
O A:HIS349 4.6 9.4 1.0
C A:CYS320 4.7 22.1 1.0
O A:CYS320 4.7 16.0 1.0
O A:CYS318 4.8 28.7 1.0
CB A:VAL322 4.8 15.7 1.0
C A:HIS349 4.8 19.6 1.0
C A:VAL322 4.9 23.0 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 Dec 16 03:49:23 2020

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