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Zinc in PDB 6ygy: Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-4-[2-(4-Methylphenyl)Ethyl]-1,7- Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One

Enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-4-[2-(4-Methylphenyl)Ethyl]-1,7- Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-4-[2-(4-Methylphenyl)Ethyl]-1,7- Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-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-4-[2-(4-Methylphenyl)Ethyl]-1,7- Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 6ygy 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) 37.77 / 1.52
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 85.224, 65.050, 71.561, 90.00, 94.28, 90.00
R / Rfree (%) 14.5 / 18.2

Other elements in 6ygy:

The structure of Trna-Guanine Transglycosylase (Tgt) Labeled with 5-Fluorotryptophan in Co-Crystallized Complex with 6-Amino-4-[2-(4-Methylphenyl)Ethyl]-1,7- Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-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-4-[2-(4-Methylphenyl)Ethyl]-1,7- Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One (pdb code 6ygy). 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-4-[2-(4-Methylphenyl)Ethyl]-1,7- Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 6ygy:

Zinc binding site 1 out of 1 in 6ygy

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

b:25.9
occ:1.00
 ND1 A:HIS349 2.2 24.0 1.0
SG A:CYS323 2.3 24.8 1.0
SG A:CYS320 2.3 29.3 1.0
SG A:CYS318 2.3 27.9 1.0
CE1 A:HIS349 3.0 24.2 1.0
HB3 A:CYS318 3.0 33.4 1.0
HE1 A:HIS349 3.0 29.0 1.0
HB2 A:CYS323 3.1 32.3 1.0
HB3 A:CYS320 3.2 37.5 1.0
CB A:CYS318 3.3 27.9 1.0
CB A:CYS323 3.3 26.9 1.0
CG A:HIS349 3.3 23.1 1.0
H A:CYS323 3.4 33.5 1.0
HB2 A:HIS349 3.4 29.3 1.0
CB A:CYS320 3.4 31.2 1.0
H A:CYS320 3.5 41.5 1.0
HA A:HIS349 3.6 30.7 1.0
HB2 A:CYS318 3.7 33.4 1.0
CB A:HIS349 3.8 24.4 1.0
HB A:VAL322 3.9 34.5 1.0
N A:CYS323 4.0 27.9 1.0
HB3 A:CYS323 4.0 32.3 1.0
HB2 A:LEU314 4.1 25.7 1.0
HB2 A:CYS320 4.2 37.5 1.0
CA A:HIS349 4.2 25.6 1.0
N A:CYS320 4.2 34.6 1.0
NE2 A:HIS349 4.2 23.2 1.0
CA A:CYS323 4.3 28.5 1.0
CA A:CYS320 4.3 33.3 1.0
CD2 A:HIS349 4.4 23.3 1.0
HD12 A:LEU314 4.5 27.1 1.0
HE22 A:GLN356 4.5 40.2 1.0
HB3 A:ASP315 4.5 32.7 1.0
O A:HIS349 4.5 24.5 1.0
H A:ASP315 4.5 27.6 1.0
HB3 A:ALA352 4.5 35.7 1.0
CA A:CYS318 4.6 30.0 1.0
HA A:CYS323 4.7 34.2 1.0
HB3 A:HIS349 4.7 29.3 1.0
O A:CYS320 4.7 33.8 1.0
C A:CYS320 4.7 34.0 1.0
C A:CYS318 4.7 33.1 1.0
H A:VAL322 4.8 38.5 1.0
C A:HIS349 4.8 24.9 1.0
CB A:VAL322 4.8 28.7 1.0
O A:CYS318 4.9 32.3 1.0
HE2 A:HIS349 4.9 27.9 1.0
C A:VAL322 5.0 28.7 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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