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Zinc in PDB 2qzr: Trna-Guanine Transglycosylase(Tgt) in Complex with 6-Amino-2-[(1- Naphthylmethyl)Amino]-3,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One

Enzymatic activity of Trna-Guanine Transglycosylase(Tgt) in Complex with 6-Amino-2-[(1- Naphthylmethyl)Amino]-3,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One

All present enzymatic activity of Trna-Guanine Transglycosylase(Tgt) in Complex with 6-Amino-2-[(1- Naphthylmethyl)Amino]-3,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One:
2.4.2.29;

Protein crystallography data

The structure of Trna-Guanine Transglycosylase(Tgt) in Complex with 6-Amino-2-[(1- Naphthylmethyl)Amino]-3,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 2qzr was solved by S.R.Hoertner, T.Ritschel, B.Stengl, C.Kramer, W.B.Schweizer, B.Wagner, M.Kansy, G.Klebe, F.Diederich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 88.085, 63.440, 71.123, 90.00, 93.30, 90.00
R / Rfree (%) 19.8 / 25.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase(Tgt) in Complex with 6-Amino-2-[(1- Naphthylmethyl)Amino]-3,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One (pdb code 2qzr). 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-2-[(1- Naphthylmethyl)Amino]-3,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One, PDB code: 2qzr:

Zinc binding site 1 out of 1 in 2qzr

Go back to Zinc Binding Sites List in 2qzr
Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase(Tgt) in Complex with 6-Amino-2-[(1- Naphthylmethyl)Amino]-3,7-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) in Complex with 6-Amino-2-[(1- Naphthylmethyl)Amino]-3,7-Dihydro-8H-Imidazo[4,5-G]Quinazolin-8-One within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:20.6
occ:1.00
 ND1 A:HIS349 2.1 21.2 1.0
SG A:CYS318 2.2 23.3 1.0
SG A:CYS320 2.3 18.0 1.0
SG A:CYS323 2.3 18.0 1.0
CE1 A:HIS349 2.9 21.4 1.0
CB A:CYS318 3.1 17.7 1.0
CG A:HIS349 3.2 12.2 1.0
CB A:CYS323 3.2 14.5 1.0
CB A:CYS320 3.4 20.0 1.0
CB A:HIS349 3.6 10.2 1.0
N A:CYS323 3.9 21.4 1.0
CA A:HIS349 4.0 14.3 1.0
NE2 A:HIS349 4.1 13.5 1.0
N A:CYS320 4.1 24.5 1.0
CA A:CYS323 4.1 18.9 1.0
CA A:CYS320 4.2 20.9 1.0
CD2 A:HIS349 4.2 19.2 1.0
CA A:CYS318 4.4 21.3 1.0
O A:HIS349 4.5 14.4 1.0
C A:CYS318 4.6 16.2 1.0
O A:CYS320 4.6 21.1 1.0
C A:CYS320 4.7 20.2 1.0
C A:HIS349 4.7 21.6 1.0
CB A:VAL322 4.7 13.9 1.0
O A:CYS318 4.8 25.2 1.0
C A:VAL322 4.8 20.6 1.0

Reference:

S.R.Hortner, T.Ritschel, B.Stengl, C.Kramer, W.B.Schweizer, B.Wagner, M.Kansy, G.Klebe, F.Diederich. Potent Inhibitors of Trna-Guanine Transglycosylase, An Enzyme Linked to the Pathogenicity of the Shigella Bacterium: Charge-Assisted Hydrogen Bonding. Angew.Chem.Int.Ed.Engl. V. 46 8266 2007.
ISSN: ISSN 1433-7851
PubMed: 17902085
DOI: 10.1002/ANIE.200702961
Page generated: Thu Oct 17 03:38:04 2024

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