Zinc in PDB 6yry: Trna-Guanine Transglycosylase (Tgt) H333A Mutant Crystallised at pH 5.5

All present enzymatic activity of Trna-Guanine Transglycosylase (Tgt) H333A Mutant Crystallised at pH 5.5:
2.4.2.29;

The structure of Trna-Guanine Transglycosylase (Tgt) H333A Mutant Crystallised at pH 5.5, PDB code: 6yry was solved by A.Nguyen, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.87 / 1.82
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.315, 65.147, 70.891, 90.00, 96.48, 90.00
R / Rfree (%)	17.5 / 20.4

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (Tgt) H333A Mutant Crystallised at pH 5.5 (pdb code 6yry). 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) H333A Mutant Crystallised at pH 5.5, PDB code: 6yry:

Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase (Tgt) H333A Mutant Crystallised at pH 5.5


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 (Tgt) H333A Mutant Crystallised at pH 5.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn404 b:22.7 occ:0.91 ND1 A:HIS349 2.1 18.7 1.0 SG A:CYS320 2.3 21.6 1.0 SG A:CYS318 2.3 22.6 1.0 SG A:CYS323 2.4 20.6 1.0 CE1 A:HIS349 2.9 22.0 1.0 CB A:CYS318 3.2 22.4 1.0 CG A:HIS349 3.3 17.6 1.0 CB A:CYS323 3.3 17.8 1.0 CB A:CYS320 3.3 18.9 1.0 CB A:HIS349 3.7 19.3 1.0 N A:CYS323 3.9 20.7 1.0 N A:CYS320 4.0 20.7 1.0 CA A:HIS349 4.1 18.1 1.0 NE2 A:HIS349 4.1 22.1 1.0 CA A:CYS320 4.2 23.3 1.0 CA A:CYS323 4.2 19.2 1.0 CD2 A:HIS349 4.3 19.8 1.0 CA A:CYS318 4.5 25.9 1.0 O A:HIS349 4.5 21.2 1.0 C A:CYS318 4.6 28.9 1.0 C A:CYS320 4.7 23.0 1.0 O A:CYS320 4.7 22.6 1.0 C A:HIS349 4.8 18.3 1.0 O A:CYS318 4.8 26.5 1.0 CB A:VAL322 4.9 20.3 1.0 C A:VAL322 5.0 20.3 1.0

A.Nguyen, A.Heine, G.Klebe. Mutation Study on Trna-Guanine Transglycosylase For Catalysis Testing To Be Published.