Atomistry » Zinc » PDB 6zxw-7a8r » 7a6d
Atomistry »
  Zinc »
    PDB 6zxw-7a8r »
      7a6d »

Zinc in PDB 7a6d: Trna-Guanine Transglycosylase C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol

Enzymatic activity of Trna-Guanine Transglycosylase C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol

All present enzymatic activity of Trna-Guanine Transglycosylase C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol, PDB code: 7a6d was solved by D.Nguyen, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.79 / 1.59
Space group P 65 2 2
Cell size a, b, c (Å), α, β, γ (°) 127.868, 127.868, 115.189, 90, 90, 120
R / Rfree (%) 14.8 / 17.8

Other elements in 7a6d:

The structure of Trna-Guanine Transglycosylase C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol (pdb code 7a6d). 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 C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol, PDB code: 7a6d:

Zinc binding site 1 out of 1 in 7a6d

Go back to Zinc Binding Sites List in 7a6d
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol


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 C158S/C281S/Y330C/H333A Mutant in Complex with Rac-Trans-4,4-Difluorocyclopentane-1,2-Diol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:20.4
occ:1.00
ND1 A:HIS349 2.1 18.0 1.0
SG A:CYS318 2.3 21.0 1.0
SG A:CYS320 2.3 20.5 1.0
SG A:CYS323 2.3 21.5 1.0
CE1 A:HIS349 2.9 21.2 1.0
HE1 A:HIS349 3.0 25.4 1.0
HB2 A:CYS323 3.0 25.3 1.0
HB3 A:CYS318 3.0 26.1 1.0
HB3 A:CYS320 3.2 25.0 1.0
CG A:HIS349 3.2 18.5 1.0
CB A:CYS318 3.3 21.8 1.0
CB A:CYS323 3.3 21.1 1.0
HB2 A:HIS349 3.3 21.6 1.0
H A:CYS323 3.3 26.1 1.0
CB A:CYS320 3.4 20.9 1.0
H A:CYS320 3.4 24.4 0.5
H A:CYS320 3.5 24.4 0.5
HA A:HIS349 3.6 20.5 1.0
CB A:HIS349 3.7 18.0 1.0
HB2 A:CYS318 3.7 26.1 1.0
HB A:VAL322 3.9 25.4 1.0
N A:CYS323 3.9 21.7 1.0
HB3 A:CYS323 4.0 25.3 1.0
NE2 A:HIS349 4.1 20.2 1.0
CA A:HIS349 4.1 17.1 1.0
N A:CYS320 4.1 20.3 1.0
HB2 A:CYS320 4.1 25.0 1.0
CA A:CYS323 4.2 22.0 1.0
CD2 A:HIS349 4.2 19.9 1.0
CA A:CYS320 4.2 20.8 1.0
HB2 A:LEU314 4.3 23.5 1.0
O A:HIS349 4.5 17.9 1.0
HE22 A:GLN356 4.5 33.2 1.0
HB3 A:ASP315 4.5 27.8 1.0
HD12 A:LEU314 4.5 25.2 1.0
HB3 A:ALA352 4.5 22.1 1.0
CA A:CYS318 4.5 21.4 1.0
HA A:CYS323 4.5 26.4 1.0
HB3 A:HIS349 4.6 21.6 1.0
H A:ASP315 4.6 26.4 1.0
C A:CYS318 4.6 20.7 1.0
C A:HIS349 4.7 18.1 1.0
C A:CYS320 4.7 22.4 1.0
HB2 A:PHE353 4.7 24.5 1.0
O A:CYS320 4.7 21.2 1.0
O A:CYS318 4.8 23.0 1.0
H A:VAL322 4.8 26.1 1.0
CB A:VAL322 4.8 21.1 1.0
HE2 A:HIS349 4.8 24.2 1.0
C A:VAL322 4.9 22.7 1.0

Reference:

D.Nguyen, X.Xie, S.Jakobi, F.Terwesten, A.Metz, T.X.P.Nguyen, V.A.Palchykov, A.Heine, K.Reuter, G.Klebe. Targeting A Cryptic Pocket in A Protein-Protein Contact By Disulfide-Induced Rupture of A Homodimeric Interface Acs Chem.Biol. 2021.
ISSN: ESSN 1554-8937
DOI: 10.1021/ACSCHEMBIO.1C00296
Page generated: Tue Oct 29 16:20:26 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy