Zinc in PDB 2pwu: Trna Guanine Transglycosylase in Complex with Guanine

All present enzymatic activity of Trna Guanine Transglycosylase in Complex with Guanine:
2.4.2.29;

The structure of Trna Guanine Transglycosylase in Complex with Guanine, PDB code: 2pwu was solved by N.Tidten, A.Heine, K.Reuter, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.77
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.151, 64.503, 70.769, 90.00, 92.79, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Trna Guanine Transglycosylase in Complex with Guanine (pdb code 2pwu). 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 in Complex with Guanine, PDB code: 2pwu:

Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase in Complex with Guanine


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 in Complex with Guanine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:23.5 occ:1.00 ND1 A:HIS349 2.1 20.6 1.0 SG A:CYS323 2.3 23.5 1.0 SG A:CYS318 2.3 24.9 1.0 SG A:CYS320 2.4 22.7 1.0 CE1 A:HIS349 2.9 25.1 1.0 CB A:CYS318 3.2 32.2 1.0 CB A:CYS323 3.3 28.5 1.0 CG A:HIS349 3.3 24.7 1.0 CB A:CYS320 3.5 20.1 1.0 CB A:HIS349 3.7 22.7 1.0 N A:CYS323 4.0 21.9 1.0 NE2 A:HIS349 4.1 21.7 1.0 CA A:HIS349 4.1 23.1 1.0 N A:CYS320 4.1 23.3 1.0 CA A:CYS323 4.2 23.7 1.0 CA A:CYS320 4.3 26.8 1.0 CD2 A:HIS349 4.3 24.6 1.0 CA A:CYS318 4.5 28.2 1.0 O A:HIS349 4.5 16.2 1.0 C A:CYS318 4.6 26.9 1.0 O A:CYS320 4.7 24.6 1.0 C A:CYS320 4.7 24.3 1.0 C A:HIS349 4.8 21.1 1.0 CB A:VAL322 4.8 23.0 1.0 O A:CYS318 4.9 26.1 1.0 CB A:LEU314 5.0 27.6 1.0 C A:VAL322 5.0 17.1 1.0

N.Tidten, B.Stengl, A.Heine, G.A.Garcia, G.Klebe, K.Reuter. Glutamate Versus Glutamine Exchange Swaps Substrate Selectivity in Trna-Guanine Transglycosylase: Insight Into the Regulation of Substrate Selectivity By Kinetic and Crystallographic Studies. J.Mol.Biol. V. 374 764 2007.
ISSN: ISSN 0022-2836
PubMed: 17949745
DOI: 10.1016/J.JMB.2007.09.062