Zinc in PDB 1wkd: Trna-Guanine Transglycosylase

All present enzymatic activity of Trna-Guanine Transglycosylase:
2.4.2.29;

The structure of Trna-Guanine Transglycosylase, PDB code: 1wkd was solved by C.Romier, K.Reuter, D.Suck, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 2.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.700, 63.700, 72.500, 90.00, 96.40, 90.00
R / Rfree (%)	20.4 / 27.6

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase (pdb code 1wkd). 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, PDB code: 1wkd:

Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:31.2 occ:1.00 SG A:CYS323 1.8 29.7 1.0 SG A:CYS318 2.1 27.8 1.0 ND1 A:HIS349 2.5 14.9 1.0 SG A:CYS320 2.5 27.2 1.0 CB A:CYS323 3.2 31.6 1.0 CE1 A:HIS349 3.3 12.8 1.0 CB A:CYS318 3.3 38.1 1.0 CB A:CYS320 3.4 33.4 1.0 CG A:HIS349 3.6 16.5 1.0 N A:CYS323 3.8 41.6 1.0 CB A:HIS349 4.0 13.7 1.0 N A:CYS320 4.0 43.5 1.0 CA A:CYS323 4.1 35.5 1.0 CA A:CYS320 4.2 38.0 1.0 CA A:HIS349 4.2 12.4 1.0 O A:CYS320 4.3 31.6 1.0 O A:CYS318 4.4 41.6 1.0 NE2 A:HIS349 4.5 12.0 1.0 C A:CYS320 4.5 36.2 1.0 C A:CYS318 4.5 43.3 1.0 CA A:CYS318 4.5 40.1 1.0 CD2 A:HIS349 4.6 14.8 1.0 CB A:VAL322 4.8 38.5 1.0 O A:HIS349 4.8 14.7 1.0 C A:VAL322 4.8 41.9 1.0 CB A:LEU314 5.0 17.4 1.0 C A:HIS349 5.0 12.9 1.0

C.Romier, K.Reuter, D.Suck, R.Ficner. Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna-Guanine Transglycosylase Reveal Aspartate 102 As the Active Site Nucleophile. Biochemistry V. 35 15734 1996.
ISSN: ISSN 0006-2960
PubMed: 8961936
DOI: 10.1021/BI962003N