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Zinc in PDB 1y5v: Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One

Enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 1y5v was solved by B.Stengl, E.A.Meyer, A.Heine, R.Brenk, F.Diederich, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.58
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.590, 64.930, 70.120, 90.00, 95.83, 90.00
R / Rfree (%) 17 / 21.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One (pdb code 1y5v). 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 (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 1y5v:

Zinc binding site 1 out of 1 in 1y5v

Go back to Zinc Binding Sites List in 1y5v
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One


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 (Tgt) in Complex with 6-Amino-4-(2- Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:14.6
occ:1.00
 ND1 A:HIS349 2.2 14.9 1.0
SG A:CYS323 2.3 14.5 1.0
SG A:CYS320 2.3 15.3 1.0
SG A:CYS318 2.3 18.3 1.0
CE1 A:HIS349 3.0 16.9 1.0
CB A:CYS323 3.2 12.0 1.0
CB A:CYS318 3.3 16.6 1.0
CG A:HIS349 3.3 13.7 1.0
CB A:CYS320 3.4 13.4 1.0
CB A:HIS349 3.8 11.8 1.0
N A:CYS323 3.9 12.4 1.0
N A:CYS320 4.1 18.0 1.0
CA A:HIS349 4.2 11.8 1.0
CA A:CYS323 4.2 14.4 1.0
NE2 A:HIS349 4.2 16.1 1.0
CA A:CYS320 4.2 15.5 1.0
CD2 A:HIS349 4.4 16.0 1.0
O A:HIS349 4.5 13.3 1.0
CA A:CYS318 4.6 17.3 1.0
C A:CYS320 4.6 14.4 1.0
C A:CYS318 4.7 17.1 1.0
O A:CYS320 4.7 15.7 1.0
CB A:VAL322 4.8 13.4 1.0
C A:HIS349 4.8 13.6 1.0
O A:CYS318 4.9 21.3 1.0
C A:VAL322 4.9 13.4 1.0

Reference:

B.Stengl, E.A.Meyer, A.Heine, R.Brenk, F.Diederich, G.Klebe. Crystal Structures of Trna-Guanine Transglycosylase (Tgt) in Complex with Novel and Potent Inhibitors Unravel Pronounced Induced-Fit Adaptations and Suggest Dimer Formation Upon Substrate Binding J.Mol.Biol. V. 370 492 2007.
ISSN: ISSN 0022-2836
PubMed: 17524419
DOI: 10.1016/J.JMB.2007.04.008
Page generated: Wed Oct 16 20:45:52 2024

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