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Zinc in PDB 6ygx: Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One

Enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One, PDB code: 6ygx 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) 42.60 / 1.35
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 85.083, 64.980, 71.374, 90.00, 93.78, 90.00
R / Rfree (%) 13.5 / 15.6

Other elements in 6ygx:

The structure of Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One (pdb code 6ygx). 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) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One, PDB code: 6ygx:

Zinc binding site 1 out of 1 in 6ygx

Go back to Zinc Binding Sites List in 6ygx
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-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) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-2-(Methylamino)-4-(2-((2R,3R,4S, 5R,6S)-3,4,5,6-Tetramethoxytetrahydro-2H-Pyran-2-Yl)Ethyl)-1H- Imidazo[4,5-G]Quinazolin-8(7H)-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:21.1
occ:0.63
SG A:CYS323 2.3 29.0 1.0
ND1 A:HIS349 2.3 21.4 1.0
SG A:CYS318 2.3 30.4 1.0
SG A:CYS320 2.4 33.3 1.0
HB3 A:CYS318 3.0 40.0 1.0
HE1 A:HIS349 3.0 26.9 1.0
CE1 A:HIS349 3.0 22.4 1.0
HB3 A:CYS320 3.1 42.1 1.0
HB2 A:CYS323 3.1 38.1 1.0
CB A:CYS318 3.2 33.3 1.0
H A:CYS323 3.3 41.4 1.0
CB A:CYS323 3.3 31.7 1.0
CB A:CYS320 3.3 35.1 1.0
CG A:HIS349 3.5 20.1 1.0
H A:CYS320 3.5 47.4 1.0
HB2 A:CYS318 3.6 40.0 1.0
HB2 A:HIS349 3.6 24.7 1.0
HA A:HIS349 3.6 24.5 1.0
HB A:VAL322 3.8 44.4 1.0
N A:CYS323 3.9 34.5 1.0
CB A:HIS349 3.9 20.6 1.0
HB3 A:CYS323 4.0 38.1 1.0
HB2 A:LEU314 4.1 30.5 1.0
HB2 A:CYS320 4.1 42.1 1.0
N A:CYS320 4.2 39.5 1.0
CA A:CYS320 4.2 38.2 1.0
CA A:CYS323 4.2 34.5 1.0
NE2 A:HIS349 4.3 21.3 1.0
CA A:HIS349 4.3 20.4 1.0
H A:ASP315 4.4 35.2 1.0
HE22 A:GLN356 4.4 38.6 1.0
HB3 A:ASP315 4.4 41.3 1.0
CD2 A:HIS349 4.5 20.3 1.0
CA A:CYS318 4.6 37.2 1.0
O A:HIS349 4.6 20.4 1.0
HD12 A:LEU314 4.6 28.9 1.0
HA A:CYS323 4.6 41.4 1.0
C A:CYS320 4.7 39.6 1.0
HB3 A:ALA352 4.7 31.3 1.0
O A:CYS320 4.7 40.2 1.0
C A:CYS318 4.7 38.8 1.0
H A:VAL322 4.8 45.1 1.0
CB A:VAL322 4.8 37.0 1.0
HB3 A:HIS349 4.9 24.7 1.0
C A:HIS349 4.9 20.1 1.0
O A:CYS318 4.9 39.5 1.0
C A:VAL322 5.0 36.0 1.0
HE2 A:HIS349 5.0 25.5 1.0

Reference:

A.Nguyen, A.Heine, G.Klebe. Co-Crystallization, Nanoesi-Ms and 19F uc(Nmr) Reveal Dimer Disturbing Inhibitors and Conformational Changes at Dimer Contacts To Be Published.
Page generated: Tue Oct 29 11:32:52 2024

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