Atomistry » Zinc » PDB 4pog-4q1l » 4puk
Atomistry »
  Zinc »
    PDB 4pog-4q1l »
      4puk »

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

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

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

Resolution Low / High (Å) 27.30 / 1.49
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.788, 64.986, 70.987, 90.00, 96.27, 90.00
R / Rfree (%) 13.9 / 17.2

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 4puk

Go back to Zinc Binding Sites List in 4puk
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-2- (Methylamino)-1H,7H,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-2- (Methylamino)-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:17.3
occ:1.00
ND1 A:HIS349 2.1 15.6 1.0
SG A:CYS320 2.3 17.0 1.0
SG A:CYS318 2.3 19.0 1.0
SG A:CYS323 2.3 17.3 1.0
CE1 A:HIS349 2.9 16.3 1.0
CB A:CYS323 3.3 16.8 1.0
CG A:HIS349 3.3 14.3 1.0
CB A:CYS318 3.3 19.7 1.0
CB A:CYS320 3.4 17.2 1.0
CB A:HIS349 3.8 13.7 1.0
N A:CYS323 3.9 15.8 1.0
CA A:HIS349 4.1 13.4 1.0
N A:CYS320 4.1 20.3 1.0
NE2 A:HIS349 4.2 16.2 1.0
CA A:CYS323 4.2 16.8 1.0
CA A:CYS320 4.2 18.6 1.0
CD2 A:HIS349 4.3 15.2 1.0
O A:HIS349 4.6 13.8 1.0
CA A:CYS318 4.6 19.4 1.0
C A:CYS320 4.7 18.4 1.0
O A:CYS320 4.7 17.7 1.0
C A:CYS318 4.7 21.5 1.0
CB A:VAL322 4.8 15.8 1.0
C A:HIS349 4.8 13.5 1.0
O A:CYS318 4.8 22.4 1.0
C A:VAL322 4.9 16.8 1.0

Reference:

M.Neeb, P.Czodrowski, A.Heine, L.J.Barandun, C.Hohn, F.Diederich, G.Klebe. Chasing Protons: How Isothermal Titration Calorimetry, Mutagenesis, and Pka Calculations Trace the Locus of Charge in Ligand Binding to A Trna-Binding Enzyme. J.Med.Chem. V. 57 5554 2014.
ISSN: ISSN 0022-2623
PubMed: 24955548
DOI: 10.1021/JM500401X
Page generated: Sun Oct 27 06:05:13 2024

Last articles

Zn in 9FD2
Zn in 9GUW
Zn in 9GUX
Zn in 9F7C
Zn in 9GUR
Zn in 9F7A
Zn in 9DDE
Zn in 9DBY
Zn in 9EBZ
Zn in 9DGG
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy