Atomistry » Zinc » PDB 4q30-4q8u » 4q4m
Atomistry »
  Zinc »
    PDB 4q30-4q8u »
      4q4m »

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

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