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Zinc in PDB 3c2y: Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-2-Methyl- 1,7-Dihydro-Imidazo[4,5-G]Quinazolin-8-One

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

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-2-Methyl- 1,7-Dihydro-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-2-Methyl- 1,7-Dihydro-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 3c2y was solved by T.Ritschel, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.78
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.300, 64.800, 70.300, 90.00, 96.00, 90.00
R / Rfree (%) 16.4 / 21.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-2-Methyl- 1,7-Dihydro-Imidazo[4,5-G]Quinazolin-8-One (pdb code 3c2y). 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-2-Methyl- 1,7-Dihydro-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 3c2y:

Zinc binding site 1 out of 1 in 3c2y

Go back to Zinc Binding Sites List in 3c2y
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-2-Methyl- 1,7-Dihydro-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-2-Methyl- 1,7-Dihydro-Imidazo[4,5-G]Quinazolin-8-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn390

b:11.8
occ:1.00
 ND1 A:HIS349 2.2 10.8 1.0
SG A:CYS318 2.3 13.7 1.0
SG A:CYS323 2.3 12.6 1.0
SG A:CYS320 2.3 13.6 1.0
CE1 A:HIS349 3.0 14.7 1.0
CB A:CYS318 3.2 15.6 1.0
CB A:CYS323 3.2 11.3 1.0
CG A:HIS349 3.3 8.0 1.0
CB A:CYS320 3.3 9.4 1.0
CB A:HIS349 3.7 16.1 1.0
N A:CYS323 3.9 9.8 1.0
N A:CYS320 4.1 11.4 1.0
CA A:HIS349 4.1 8.1 1.0
NE2 A:HIS349 4.2 15.3 1.0
CA A:CYS323 4.2 6.2 1.0
CA A:CYS320 4.2 8.4 1.0
CD2 A:HIS349 4.3 8.0 1.0
O A:HIS349 4.5 9.2 1.0
CA A:CYS318 4.5 12.4 1.0
C A:CYS320 4.6 8.2 1.0
C A:CYS318 4.7 15.5 1.0
O A:CYS320 4.7 10.8 1.0
C A:HIS349 4.8 9.6 1.0
O A:CYS318 4.9 16.6 1.0
CB A:VAL322 4.9 15.0 1.0
C A:VAL322 5.0 12.7 1.0

Reference:

T.Ritschel, S.Hoertner, A.Heine, F.Diederich, G.Klebe. Crystal Structure Analysis and in Silico Pka Calculations Suggest Strong Pka Shifts of Ligands As Driving Force For High-Affinity Binding to Tgt Chembiochem V. 10 716 2009.
ISSN: ISSN 1439-4227
PubMed: 19199329
DOI: 10.1002/CBIC.200800782
Page generated: Wed Dec 16 04:10:02 2020

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