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Zinc in PDB 1p0b: Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0

Enzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0

All present enzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0:
2.4.2.29;

Protein crystallography data

The structure of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0, PDB code: 1p0b 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) 20.00 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.620, 65.540, 70.330, 90.00, 96.46, 90.00
R / Rfree (%) 17.6 / 20

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0 (pdb code 1p0b). 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 Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0, PDB code: 1p0b:

Zinc binding site 1 out of 1 in 1p0b

Go back to Zinc Binding Sites List in 1p0b
Zinc binding site 1 out of 1 in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0


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 Trna-Guanine Transglycosylase (Tgt) From Zymomonas Mobilis Complexed with Archaeosine Precursor, PREQ0 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:18.7
occ:1.00
 ND1 A:HIS349 2.1 16.8 1.0
SG A:CYS320 2.3 15.7 1.0
SG A:CYS318 2.3 18.7 1.0
SG A:CYS323 2.3 17.4 1.0
CE1 A:HIS349 2.9 16.4 1.0
CB A:CYS318 3.2 20.0 1.0
CG A:HIS349 3.3 14.8 1.0
CB A:CYS320 3.3 16.3 1.0
CB A:CYS323 3.3 16.9 1.0
CB A:HIS349 3.7 15.3 1.0
N A:CYS323 3.9 17.7 1.0
CA A:HIS349 4.1 14.6 1.0
N A:CYS320 4.1 18.4 1.0
NE2 A:HIS349 4.1 15.6 1.0
CA A:CYS320 4.2 17.4 1.0
CA A:CYS323 4.2 17.2 1.0
CD2 A:HIS349 4.3 16.7 1.0
O A:HIS349 4.5 12.5 1.0
CA A:CYS318 4.5 20.7 1.0
O A:CYS320 4.6 16.6 1.0
C A:CYS318 4.6 21.3 1.0
C A:CYS320 4.6 16.9 1.0
C A:HIS349 4.7 14.7 1.0
CB A:VAL322 4.7 17.4 1.0
O A:CYS318 4.8 20.5 1.0
C A:VAL322 4.9 17.8 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 22:15:09 2025

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