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Zinc in PDB 1pxg: Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1

Enzymatic activity of Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1

All present enzymatic activity of Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1:
2.4.2.29;

Protein crystallography data

The structure of Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1, PDB code: 1pxg was solved by J.D.Kittendorf, T.Sgraja, K.Reuter, G.Klebe, G.A.Garcia, 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 (°) 91.280, 64.940, 70.200, 90.00, 96.12, 90.00
R / Rfree (%) 15.9 / 20.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1 (pdb code 1pxg). 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 Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1, PDB code: 1pxg:

Zinc binding site 1 out of 1 in 1pxg

Go back to Zinc Binding Sites List in 1pxg
Zinc binding site 1 out of 1 in the Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Mutated Trna-Guanine Transglycosylase (Tgt) D280E Complexed with PREQ1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:14.1
occ:1.00
ND1 A:HIS349 2.1 15.6 1.0
SG A:CYS320 2.3 14.5 1.0
SG A:CYS323 2.3 14.7 1.0
SG A:CYS318 2.3 15.3 1.0
CE1 A:HIS349 2.9 12.5 1.0
CB A:CYS318 3.3 15.6 1.0
CB A:CYS323 3.3 13.3 1.0
CG A:HIS349 3.3 10.6 1.0
CB A:CYS320 3.4 12.0 1.0
CB A:HIS349 3.8 12.2 1.0
N A:CYS323 3.9 14.9 1.0
CA A:HIS349 4.1 13.4 1.0
NE2 A:HIS349 4.1 13.5 1.0
N A:CYS320 4.1 15.2 1.0
CA A:CYS323 4.2 12.3 1.0
CA A:CYS320 4.2 14.3 1.0
CD2 A:HIS349 4.3 15.6 1.0
CA A:CYS318 4.6 15.0 1.0
O A:HIS349 4.6 13.1 1.0
O A:CYS320 4.6 15.1 1.0
C A:CYS320 4.6 14.8 1.0
C A:CYS318 4.7 14.4 1.0
O A:CYS318 4.8 18.2 1.0
C A:HIS349 4.8 12.5 1.0
CB A:VAL322 4.8 11.6 1.0
C A:VAL322 4.9 17.0 1.0

Reference:

J.D.Kittendorf, T.Sgraja, K.Reuter, G.Klebe, G.A.Garcia. An Essential Role For Aspartate 264 in Catalysis By Trna-Guanine Transglycosylase From Escherichia Coli. J.Biol.Chem. V. 278 42369 2003.
ISSN: ISSN 0021-9258
PubMed: 12909636
DOI: 10.1074/JBC.M304323200
Page generated: Wed Dec 16 03:01:08 2020

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