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Zinc in PDB 1p0e: Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5

Enzymatic activity of Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5

All present enzymatic activity of Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5:
2.4.2.29;

Protein crystallography data

The structure of Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5, PDB code: 1p0e was solved by R.Brenk, M.T.Stubbs, 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) 25.00 / 2.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 64.470, 91.870, 165.830, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 25.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5 (pdb code 1p0e). 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 Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5, PDB code: 1p0e:

Zinc binding site 1 out of 1 in 1p0e

Go back to Zinc Binding Sites List in 1p0e
Zinc binding site 1 out of 1 in the Crystal Structure of Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5


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 Zymomonas Mobilis Trna-Guanine Transglycosylase (Tgt) Cocrystallised with PREQ1 at pH 5.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:23.9
occ:1.00
 ND1 A:HIS349 2.2 25.1 1.0
SG A:CYS323 2.2 23.7 1.0
SG A:CYS318 2.3 23.2 1.0
SG A:CYS320 2.4 18.3 1.0
CE1 A:HIS349 3.0 24.1 1.0
CB A:CYS323 3.1 21.1 1.0
CB A:CYS318 3.2 28.9 1.0
CG A:HIS349 3.3 24.6 1.0
CB A:CYS320 3.5 18.4 1.0
CB A:HIS349 3.8 23.0 1.0
N A:CYS323 3.9 24.2 1.0
CA A:CYS323 4.1 26.9 1.0
CA A:HIS349 4.1 23.3 1.0
N A:CYS320 4.1 23.9 1.0
NE2 A:HIS349 4.2 30.0 1.0
CA A:CYS320 4.3 21.2 1.0
CD2 A:HIS349 4.4 26.1 1.0
CA A:CYS318 4.5 29.2 1.0
O A:CYS320 4.6 22.9 1.0
O A:HIS349 4.6 24.7 1.0
C A:CYS318 4.6 30.4 1.0
C A:CYS320 4.7 20.7 1.0
O A:CYS318 4.7 34.7 1.0
CB A:VAL322 4.8 20.5 1.0
C A:HIS349 4.8 24.2 1.0
C A:VAL322 4.8 22.2 1.0
CB A:LEU314 4.9 22.7 1.0

Reference:

R.Brenk, M.T.Stubbs, A.Heine, K.Reuter, G.Klebe. Flexible Adaptations in the Structure of the Trna-Modifying Enzyme Trna-Guanine Transglycosylase and Their Implications For Substrate Selectivity, Reaction Mechanism and Structure-Based Drug Design Chembiochem V. 4 1066 2003.
ISSN: ISSN 1439-4227
PubMed: 14523925
DOI: 10.1002/CBIC.200300644
Page generated: Tue Aug 19 22:15:39 2025

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