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Zinc in PDB 4q4m: Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-One

Enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-One

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-One:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-One, PDB code: 4q4m 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) 26.84 / 1.62
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.511, 63.887, 70.399, 90.00, 92.99, 90.00
R / Rfree (%) 15.7 / 18.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-One (pdb code 4q4m). 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-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-One, PDB code: 4q4m:

Zinc binding site 1 out of 1 in 4q4m

Go back to Zinc Binding Sites List in 4q4m
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 6-Amino-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-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-4-Phenyl- 1,2-Dihydro-1,3,5-Triazin-2-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:14.4
occ:1.00
 ND1 A:HIS349 2.1 13.0 1.0
SG A:CYS323 2.3 14.1 1.0
SG A:CYS320 2.3 13.5 1.0
SG A:CYS318 2.3 16.0 1.0
CE1 A:HIS349 2.9 13.5 1.0
CB A:CYS323 3.2 12.6 1.0
CB A:CYS318 3.3 17.5 1.0
CG A:HIS349 3.3 11.4 1.0
CB A:CYS320 3.4 11.2 1.0
CB A:HIS349 3.7 11.2 1.0
N A:CYS323 3.9 12.6 1.0
NE2 A:HIS349 4.1 15.2 1.0
CA A:HIS349 4.1 9.6 1.0
N A:CYS320 4.1 16.6 1.0
CA A:CYS323 4.2 13.2 1.0
CA A:CYS320 4.2 14.2 1.0
CD2 A:HIS349 4.3 10.9 1.0
O A:HIS349 4.5 11.9 1.0
CA A:CYS318 4.6 17.1 1.0
O A:CYS320 4.7 16.2 1.0
C A:CYS320 4.7 15.1 1.0
C A:CYS318 4.7 17.4 1.0
CB A:VAL322 4.8 13.8 1.0
C A:HIS349 4.8 11.5 1.0
O A:CYS318 4.9 20.9 1.0
C A:VAL322 4.9 14.2 1.0

Reference:

M.Neeb, C.Hohn, A.Heine, F.Diederich, G.Klebe. 5-Azacytosines As A Novel Scaffold to Inhibit Z. Mobilis Tgt with Expected Improved Bioavailability and Synthetic Accessibility To Be Published.
Page generated: Sun Oct 27 06:15:02 2024

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