Zinc in PDB 4pun: Trna-Guanine Transglycosylase (Tgt) Apo-Structure pH 7.8

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) Apo-Structure pH 7.8:
2.4.2.29;

The structure of Trna-Guanine Transglycosylase (Tgt) Apo-Structure pH 7.8, PDB code: 4pun was solved by M.Neeb, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.01 / 1.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.500, 64.650, 69.930, 90.00, 95.95, 90.00
R / Rfree (%)	13.9 / 16.2

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) Apo-Structure pH 7.8 (pdb code 4pun). 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) Apo-Structure pH 7.8, PDB code: 4pun:

Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) Apo-Structure pH 7.8


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) Apo-Structure pH 7.8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:13.3 occ:1.00 ND1 A:HIS349 2.1 12.6 1.0 SG A:CYS320 2.3 13.2 1.0 SG A:CYS323 2.3 13.5 1.0 SG A:CYS318 2.3 14.6 1.0 CE1 A:HIS349 2.9 13.6 1.0 CG A:HIS349 3.2 11.9 1.0 CB A:CYS323 3.3 13.2 1.0 CB A:CYS318 3.3 15.3 1.0 CB A:CYS320 3.4 13.4 1.0 CB A:HIS349 3.7 12.4 1.0 N A:CYS323 3.9 13.5 1.0 CA A:HIS349 4.1 11.3 1.0 NE2 A:HIS349 4.1 13.3 1.0 N A:CYS320 4.2 14.6 1.0 CA A:CYS323 4.2 13.2 1.0 CA A:CYS320 4.2 13.5 1.0 CD2 A:HIS349 4.3 12.5 1.0 O A:HIS349 4.5 11.7 1.0 CA A:CYS318 4.6 15.8 1.0 O A:CYS320 4.7 14.3 1.0 C A:CYS320 4.7 13.2 1.0 C A:CYS318 4.7 16.2 1.0 C A:HIS349 4.7 11.0 1.0 CB A:VAL322 4.8 13.2 1.0 O A:CYS318 4.8 17.0 1.0 C A:VAL322 4.9 13.0 1.0

M.Neeb, P.Czodrowski, A.Heine, L.J.Barandun, C.Hohn, F.Diederich, G.Klebe. Chasing Protons: How Isothermal Titration Calorimetry, Mutagenesis, and Pka Calculations Trace the Locus of Charge in Ligand Binding to A Trna-Binding Enzyme. J.Med.Chem. V. 57 5554 2014.
ISSN: ISSN 0022-2623
PubMed: 24955548
DOI: 10.1021/JM500401X