Zinc in PDB 6ygv: Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide

Enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide, PDB code: 6ygv was solved by A.Nguyen, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.19 / 1.63
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.824, 64.911, 71.070, 90.00, 95.73, 90.00
R / Rfree (%) 13.1 / 16.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide (pdb code 6ygv). 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 Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide, PDB code: 6ygv:

Zinc binding site 1 out of 1 in 6ygv

Go back to Zinc Binding Sites List in 6ygv
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide


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 Co-Crystallized Complex with (E)-N-Ethyl-4-Oxo-4-Phenylbut-2-Enamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn406

b:21.9
occ:1.00
 ND1 A:HIS349 2.1 20.4 1.0
SG A:CYS320 2.3 21.9 1.0
SG A:CYS318 2.3 23.4 1.0
SG A:CYS323 2.3 22.4 1.0
CE1 A:HIS349 2.9 19.9 1.0
HE1 A:HIS349 3.0 23.9 1.0
HB2 A:CYS323 3.0 27.8 1.0
HB3 A:CYS318 3.0 29.2 1.0
HB3 A:CYS320 3.2 26.4 1.0
CG A:HIS349 3.3 20.1 1.0
CB A:CYS318 3.3 24.3 1.0
CB A:CYS323 3.3 23.1 1.0
H A:CYS323 3.3 26.6 1.0
HB2 A:HIS349 3.4 23.6 1.0
CB A:CYS320 3.4 21.9 1.0
H A:CYS320 3.5 29.2 1.0
HA A:HIS349 3.5 22.3 1.0
HB2 A:CYS318 3.7 29.2 1.0
CB A:HIS349 3.7 19.7 1.0
HB A:VAL322 3.9 26.6 1.0
N A:CYS323 4.0 22.1 1.0
HB3 A:CYS323 4.0 27.8 1.0
CA A:HIS349 4.1 18.6 1.0
NE2 A:HIS349 4.1 20.2 1.0
N A:CYS320 4.1 24.3 1.0
HB2 A:CYS320 4.2 26.4 1.0
HB2 A:LEU314 4.2 28.6 1.0
CA A:CYS323 4.2 24.6 1.0
CA A:CYS320 4.2 22.9 1.0
CD2 A:HIS349 4.3 21.2 1.0
HD12 A:LEU314 4.3 26.3 1.0
HB3 A:ALA352 4.5 25.2 1.0
O A:HIS349 4.5 19.7 1.0
HE22 A:GLN356 4.5 34.7 1.0
HB3 A:ASP315 4.5 33.4 1.0
CA A:CYS318 4.6 25.0 1.0
HA A:CYS323 4.6 29.6 1.0
HB3 A:HIS349 4.6 23.6 1.0
H A:ASP315 4.7 30.2 1.0
O A:CYS320 4.7 22.8 1.0
C A:CYS320 4.7 22.8 1.0
C A:CYS318 4.7 24.5 1.0
C A:HIS349 4.7 20.0 1.0
H A:VAL322 4.8 29.1 1.0
O A:CYS318 4.8 26.7 1.0
HE2 A:HIS349 4.9 24.3 1.0
CB A:VAL322 4.9 22.1 1.0
C A:VAL322 5.0 23.8 1.0

Reference:

A.Nguyen, A.Heine, G.Klebe. Ligands Disturb Dimer Contacts To Be Published.
Page generated: Wed Dec 16 13:16:09 2020

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