Zinc in PDB 2z1v: Trna Guanine Transglycosylase E235Q Mutant Apo Structure, pH 8.5

All present enzymatic activity of Trna Guanine Transglycosylase E235Q Mutant Apo Structure, pH 8.5:
2.4.2.29;

The structure of Trna Guanine Transglycosylase E235Q Mutant Apo Structure, pH 8.5, PDB code: 2z1v was solved by N.Tidten, B.Stengl, A.Heine, G.A.Garcia, G.Klebe, K.Reuter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.757, 65.175, 70.455, 90.00, 96.12, 90.00
R / Rfree (%)	14.3 / 20.3

The binding sites of Zinc atom in the Trna Guanine Transglycosylase E235Q Mutant Apo Structure, pH 8.5 (pdb code 2z1v). 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 E235Q Mutant Apo Structure, pH 8.5, PDB code: 2z1v:

Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase E235Q Mutant Apo Structure, pH 8.5


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 E235Q Mutant Apo Structure, pH 8.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:16.7 occ:1.00 ND1 A:HIS349 2.2 18.0 1.0 SG A:CYS323 2.3 18.4 1.0 SG A:CYS318 2.3 17.4 1.0 SG A:CYS320 2.3 17.6 1.0 CE1 A:HIS349 2.9 15.9 1.0 CB A:CYS318 3.2 17.8 1.0 CB A:CYS323 3.3 14.6 1.0 CG A:HIS349 3.3 15.2 1.0 CB A:CYS320 3.4 17.6 1.0 CB A:HIS349 3.8 16.7 1.0 N A:CYS323 3.9 17.6 1.0 N A:CYS320 4.1 16.6 1.0 NE2 A:HIS349 4.2 19.1 1.0 CA A:HIS349 4.2 14.6 1.0 CA A:CYS323 4.2 16.6 1.0 CA A:CYS320 4.2 16.8 1.0 CD2 A:HIS349 4.3 18.2 1.0 CA A:CYS318 4.5 18.9 1.0 O A:HIS349 4.6 15.4 1.0 C A:CYS318 4.6 17.1 1.0 O A:CYS320 4.6 17.1 1.0 C A:CYS320 4.6 15.4 1.0 O A:CYS318 4.7 23.5 1.0 CB A:VAL322 4.8 15.5 1.0 C A:HIS349 4.8 13.2 1.0 C A:VAL322 5.0 15.1 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