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Zinc in PDB 4q4q: Trna-Guanine Transglycosylase (Tgt) in Complex with 2-[(Thiophen-2- Ylmethyl)Amino]-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One

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

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 2-[(Thiophen-2- Ylmethyl)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-[(Thiophen-2- Ylmethyl)Amino]-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 4q4q 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) 25.21 / 1.41
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 91.272, 64.850, 70.427, 90.00, 96.09, 90.00
R / Rfree (%) 12.4 / 16.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Complex with 2-[(Thiophen-2- Ylmethyl)Amino]-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One (pdb code 4q4q). 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-[(Thiophen-2- Ylmethyl)Amino]-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 4q4q:

Zinc binding site 1 out of 1 in 4q4q

Go back to Zinc Binding Sites List in 4q4q
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 2-[(Thiophen-2- Ylmethyl)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-[(Thiophen-2- Ylmethyl)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:9.7
occ:1.00
 ND1 A:HIS349 2.1 7.9 1.0
SG A:CYS318 2.3 10.7 1.0
SG A:CYS320 2.3 9.4 1.0
SG A:CYS323 2.3 10.5 1.0
CE1 A:HIS349 2.9 12.2 1.0
CG A:HIS349 3.2 6.6 1.0
CB A:CYS318 3.3 10.7 1.0
CB A:CYS323 3.3 9.6 1.0
CB A:CYS320 3.4 10.6 1.0
CB A:HIS349 3.7 7.7 1.0
N A:CYS323 3.9 9.3 1.0
NE2 A:HIS349 4.0 10.2 1.0
CA A:HIS349 4.1 7.7 1.0
N A:CYS320 4.2 12.0 1.0
CA A:CYS323 4.2 11.2 1.0
CD2 A:HIS349 4.2 9.2 1.0
CA A:CYS320 4.2 12.6 1.0
O A:HIS349 4.5 8.8 1.0
CA A:CYS318 4.6 12.5 1.0
O A:CYS320 4.6 10.4 1.0
C A:CYS320 4.7 9.7 1.0
C A:CYS318 4.7 12.6 1.0
C A:HIS349 4.8 8.9 1.0
CB A:VAL322 4.8 8.5 1.0
O A:CYS318 4.9 14.5 1.0
C A:VAL322 4.9 10.8 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

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