Atomistry » Zinc » PDB 3blo-3c37 » 3c2y
Atomistry »
  Zinc »
    PDB 3blo-3c37 »
      3c2y »

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: Thu Oct 24 11:42:00 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy