Zinc in PDB 2z7k: Trna-Guanine Transglycosylase (Tgt) in Complex with 2-Amino-Lin- Benzoguanine

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) in Complex with 2-Amino-Lin- Benzoguanine:
2.4.2.29;

The structure of Trna-Guanine Transglycosylase (Tgt) in Complex with 2-Amino-Lin- Benzoguanine, PDB code: 2z7k was solved by T.Ritschel, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.28
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.500, 65.100, 70.600, 90.00, 96.20, 90.00
R / Rfree (%)	n/a / 18.6

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) in Complex with 2-Amino-Lin- Benzoguanine (pdb code 2z7k). 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 2-Amino-Lin- Benzoguanine, PDB code: 2z7k:

Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) in Complex with 2-Amino-Lin- Benzoguanine


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 2-Amino-Lin- Benzoguanine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn390 b:10.6 occ:1.00 ND1 A:HIS349 2.1 10.6 1.0 SG A:CYS323 2.3 12.2 1.0 SG A:CYS318 2.3 13.6 1.0 SG A:CYS320 2.3 11.2 1.0 CE1 A:HIS349 2.9 12.2 1.0 CB A:CYS323 3.3 11.1 1.0 CG A:HIS349 3.3 9.6 1.0 CB A:CYS318 3.3 12.9 1.0 CB A:CYS320 3.4 11.5 1.0 CB A:HIS349 3.7 10.0 1.0 N A:CYS323 3.9 10.4 1.0 N A:CYS320 4.1 13.0 1.0 CA A:HIS349 4.1 8.7 1.0 NE2 A:HIS349 4.2 12.0 1.0 CA A:CYS323 4.2 11.2 1.0 CA A:CYS320 4.2 12.6 1.0 CD2 A:HIS349 4.3 10.7 1.0 O A:HIS349 4.5 9.9 1.0 CA A:CYS318 4.6 14.7 1.0 O A:CYS320 4.7 12.6 1.0 C A:CYS320 4.7 9.8 1.0 C A:CYS318 4.7 15.0 1.0 CB A:VAL322 4.8 10.2 1.0 C A:HIS349 4.8 8.3 1.0 O A:CYS318 4.8 16.0 1.0 C A:VAL322 4.9 11.0 1.0

T.Ritschel, S.Hoertner, A.Heine, F.Diederich, G.Klebe. Crystal Structure Analysis and in Silico Pka Calculations Suggest Strong Pka Shifts of Ligands As Driving Force For High-Affinity Binding to Tgt Chembiochem V. 10 716 2009.
ISSN: ISSN 1439-4227
PubMed: 19199329
DOI: 10.1002/CBIC.200800782