Zinc in PDB 4l56: Trna Guanine Transglycosylase H333D Mutant Apo Structure

All present enzymatic activity of Trna Guanine Transglycosylase H333D Mutant Apo Structure:
2.4.2.29;

The structure of Trna Guanine Transglycosylase H333D Mutant Apo Structure, PDB code: 4l56 was solved by T.X.P.Nguyen, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.39 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.049, 65.198, 69.547, 90.00, 95.89, 90.00
R / Rfree (%)	16 / 18.4

The binding sites of Zinc atom in the Trna Guanine Transglycosylase H333D Mutant Apo Structure (pdb code 4l56). 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 H333D Mutant Apo Structure, PDB code: 4l56:

Zinc binding site 1 out of 1 in the Trna Guanine Transglycosylase H333D Mutant Apo Structure


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 H333D Mutant Apo Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:14.8 occ:1.00 ND1 A:HIS349 2.1 13.7 1.0 SG A:CYS320 2.3 17.0 1.0 SG A:CYS318 2.3 19.0 1.0 SG A:CYS323 2.3 15.3 1.0 CE1 A:HIS349 3.0 16.1 1.0 CG A:HIS349 3.2 14.8 1.0 CB A:CYS323 3.2 19.4 1.0 CB A:CYS318 3.3 19.7 1.0 CB A:CYS320 3.4 14.6 1.0 CB A:HIS349 3.6 13.7 1.0 N A:CYS323 4.0 18.1 1.0 CA A:HIS349 4.1 11.6 1.0 NE2 A:HIS349 4.1 14.9 1.0 N A:CYS320 4.1 20.5 1.0 CA A:CYS323 4.2 19.7 1.0 CA A:CYS320 4.2 18.5 1.0 CD2 A:HIS349 4.3 13.8 1.0 O A:HIS349 4.5 12.2 1.0 CA A:CYS318 4.6 22.2 1.0 C A:CYS318 4.7 23.0 1.0 C A:CYS320 4.7 18.4 1.0 C A:HIS349 4.7 11.6 1.0 O A:CYS320 4.7 20.6 1.0 CB A:VAL322 4.8 16.4 1.0 O A:CYS318 4.9 22.9 1.0 C A:VAL322 5.0 20.6 1.0

S.Jakobi, T.X.P.Nguyen, G.Klebe. What Glues A Homodimer Together: Systematic Analysis of the Stabilizing Effect of An Aromatic Hot Spot in the Protein-Protein Interface of A Trna-Modifiying Enzyme To Be Published.