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Zinc in PDB 4pum: Trna-Guanine Transglycosylase (Tgt) Mutant D156N in Complex with 6- Amino-2-(Methylamino)-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One

Enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Mutant D156N 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) Mutant D156N 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) Mutant D156N in Complex with 6- Amino-2-(Methylamino)-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 4pum 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) 70.67 / 1.93
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 89.690, 64.660, 70.770, 90.00, 93.08, 90.00
R / Rfree (%) 15.9 / 20.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) Mutant D156N in Complex with 6- Amino-2-(Methylamino)-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One (pdb code 4pum). 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) Mutant D156N in Complex with 6- Amino-2-(Methylamino)-1H,7H,8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 4pum:

Zinc binding site 1 out of 1 in 4pum

Go back to Zinc Binding Sites List in 4pum
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) Mutant D156N 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) Mutant D156N 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:19.6
occ:1.00
 ND1 A:HIS349 2.1 12.1 1.0
SG A:CYS323 2.3 14.6 1.0
SG A:CYS318 2.3 19.3 1.0
SG A:CYS320 2.4 14.7 1.0
CE1 A:HIS349 2.9 17.6 1.0
CG A:HIS349 3.2 14.5 1.0
CB A:CYS318 3.2 20.7 1.0
CB A:CYS323 3.3 13.4 1.0
CB A:CYS320 3.3 15.6 1.0
CB A:HIS349 3.6 12.3 1.0
N A:CYS323 3.9 16.3 1.0
CA A:HIS349 4.1 11.3 1.0
NE2 A:HIS349 4.1 14.6 1.0
N A:CYS320 4.2 18.4 1.0
CA A:CYS323 4.2 16.1 1.0
CA A:CYS320 4.2 21.3 1.0
CD2 A:HIS349 4.2 13.1 1.0
O A:HIS349 4.5 15.4 1.0
CA A:CYS318 4.6 23.4 1.0
O A:CYS320 4.7 19.3 1.0
C A:CYS320 4.7 19.0 1.0
C A:CYS318 4.7 19.6 1.0
C A:HIS349 4.7 11.4 1.0
CB A:VAL322 4.8 14.5 1.0
C A:VAL322 4.9 18.5 1.0
O A:CYS318 4.9 21.0 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 06:06:53 2024

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