Atomistry » Zinc » PDB 4q30-4q8u » 4q4r
Atomistry »
  Zinc »
    PDB 4q30-4q8u »
      4q4r »

Zinc in PDB 4q4r: Trna-Guanine Transglycosylase (Tgt) in Complex with 2-{[2-(Morpholin- 4-Yl)Ethyl]Amino}-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One

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

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 2-{[2-(Morpholin- 4-Yl)Ethyl]Amino}-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 2-{[2-(Morpholin- 4-Yl)Ethyl]Amino}-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 4q4r 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) 29.77 / 1.45
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.941, 64.837, 70.756, 90.00, 93.14, 90.00
R / Rfree (%) 13.6 / 17.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Complex with 2-{[2-(Morpholin- 4-Yl)Ethyl]Amino}-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One (pdb code 4q4r). 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 2-{[2-(Morpholin- 4-Yl)Ethyl]Amino}-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 4q4r:

Zinc binding site 1 out of 1 in 4q4r

Go back to Zinc Binding Sites List in 4q4r
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 2-{[2-(Morpholin- 4-Yl)Ethyl]Amino}-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 2-{[2-(Morpholin- 4-Yl)Ethyl]Amino}-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:16.6
occ:1.00
 ND1 A:HIS349 2.1 14.5 1.0
SG A:CYS323 2.3 16.5 1.0
SG A:CYS318 2.3 18.3 1.0
SG A:CYS320 2.3 15.9 1.0
CE1 A:HIS349 2.9 16.7 1.0
CG A:HIS349 3.2 14.1 1.0
CB A:CYS318 3.3 18.9 1.0
CB A:CYS323 3.3 14.8 1.0
CB A:CYS320 3.4 15.8 1.0
CB A:HIS349 3.7 14.7 1.0
N A:CYS323 3.9 15.4 1.0
NE2 A:HIS349 4.1 16.4 1.0
CA A:HIS349 4.1 14.1 1.0
N A:CYS320 4.2 18.2 1.0
CA A:CYS323 4.2 15.2 1.0
CA A:CYS320 4.2 16.4 1.0
CD2 A:HIS349 4.3 14.3 1.0
O A:HIS349 4.5 14.1 1.0
CA A:CYS318 4.6 19.8 1.0
O A:CYS320 4.7 17.6 1.0
C A:CYS320 4.7 16.8 1.0
C A:CYS318 4.7 19.9 1.0
CB A:VAL322 4.8 15.2 1.0
C A:HIS349 4.8 13.2 1.0
O A:CYS318 4.9 20.7 1.0
C A:VAL322 4.9 15.8 1.0

Reference:

M.Neeb, M.Betz, A.Heine, L.J.Barandun, C.Hohn, F.Diederich, G.Klebe. Beyond Affinity: Enthalpy-Entropy Factorization Unravels Complexity of A Flat Structure-Activity Relationship For Inhibition of A Trna-Modifying Enzyme. J.Med.Chem. V. 57 5566 2014.
ISSN: ISSN 0022-2623
PubMed: 24960372
DOI: 10.1021/JM5006868
Page generated: Sun Oct 27 06:16:03 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy