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Zinc in PDB 6ygr: Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized 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 Co-Crystallized 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 Co-Crystallized 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 Co-Crystallized Complex with 6- Amino-4-(2-Phenylethyl)-1,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 6ygr was solved by A.Nguyen, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.86 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 83.921, 65.022, 71.104, 90.00, 93.94, 90.00
R / Rfree (%) 18.2 / 22.1

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 6ygr

Go back to Zinc Binding Sites List in 6ygr
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized 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 Co-Crystallized 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:Zn401

b:20.5
occ:0.45
 SG A:CYS323 2.3 42.2 1.0
SG A:CYS320 2.3 39.4 1.0
SG A:CYS318 2.3 41.5 1.0
ND1 A:HIS349 2.4 24.0 1.0
CE1 A:HIS349 3.1 28.4 1.0
CB A:CYS318 3.3 41.9 1.0
CB A:CYS323 3.3 40.7 1.0
CB A:CYS320 3.3 36.3 1.0
CG A:HIS349 3.5 19.4 1.0
N A:CYS323 3.8 45.7 1.0
CB A:HIS349 4.0 20.3 1.0
N A:CYS320 4.1 44.7 1.0
CA A:CYS320 4.2 39.9 1.0
CA A:CYS323 4.2 47.7 1.0
NE2 A:HIS349 4.3 22.9 1.0
CA A:HIS349 4.3 19.9 1.0
O A:CYS320 4.5 41.8 1.0
CD2 A:HIS349 4.5 23.4 1.0
C A:CYS320 4.5 44.2 1.0
CA A:CYS318 4.6 52.2 1.0
CB A:VAL322 4.6 50.7 1.0
O A:HIS349 4.7 23.5 1.0
C A:CYS318 4.7 54.8 1.0
C A:VAL322 4.7 48.2 1.0
CB A:LEU314 4.8 41.2 1.0
NE2 A:GLN356 4.9 42.7 1.0
N A:ASP315 4.9 38.3 1.0
O A:CYS318 4.9 47.2 1.0
C A:HIS349 5.0 22.5 1.0

Reference:

A.Nguyen, A.Heine, G.Klebe. Co-Crystallization and Nanoesi-Ms Reveal Dimer Disturbing Inhibitors and Conformational Changes at Dimer Contacts To Be Published.
Page generated: Tue Oct 29 11:31:41 2024

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