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Zinc in PDB 1y5w: Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-[2-(4- Methylphenyl)Ethyl]-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-(4- Methylphenyl)Ethyl]-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-(4- Methylphenyl)Ethyl]-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-(4- Methylphenyl)Ethyl]-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 1y5w 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 (°) 90.920, 65.250, 69.970, 90.00, 95.98, 90.00
R / Rfree (%) 15.7 / 19.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-[2-(4- Methylphenyl)Ethyl]-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One (pdb code 1y5w). 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-(4- Methylphenyl)Ethyl]-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 1y5w:

Zinc binding site 1 out of 1 in 1y5w

Go back to Zinc Binding Sites List in 1y5w
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-[2-(4- Methylphenyl)Ethyl]-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-(4- Methylphenyl)Ethyl]-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:16.0
occ:1.00
 ND1 A:HIS349 2.2 15.0 1.0
SG A:CYS323 2.3 17.2 1.0
SG A:CYS320 2.3 16.6 1.0
SG A:CYS318 2.3 18.1 1.0
CE1 A:HIS349 3.0 14.7 1.0
CB A:CYS318 3.3 17.8 1.0
CB A:CYS323 3.3 13.4 1.0
CB A:CYS320 3.3 15.5 1.0
CG A:HIS349 3.3 11.4 1.0
CB A:HIS349 3.8 13.9 1.0
N A:CYS323 4.0 13.4 1.0
CA A:HIS349 4.1 12.9 1.0
N A:CYS320 4.2 17.6 1.0
NE2 A:HIS349 4.2 14.3 1.0
CA A:CYS320 4.2 13.9 1.0
CA A:CYS323 4.2 14.2 1.0
CD2 A:HIS349 4.4 14.7 1.0
O A:HIS349 4.5 14.1 1.0
CA A:CYS318 4.6 17.2 1.0
O A:CYS320 4.6 16.8 1.0
C A:CYS320 4.6 16.6 1.0
C A:CYS318 4.7 19.5 1.0
CB A:VAL322 4.8 15.1 1.0
O A:CYS318 4.8 23.2 1.0
C A:HIS349 4.8 13.8 1.0
C A:VAL322 4.9 17.0 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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