Zinc in PDB 1wkf: Trna-Guanine Transglycosylase

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

The structure of Trna-Guanine Transglycosylase, PDB code: 1wkf 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 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.400, 64.300, 72.000, 90.00, 97.20, 90.00
R / Rfree (%)	19.9 / 25

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

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:12.4 occ:1.00 SG A:CYS320 2.2 6.0 1.0 SG A:CYS318 2.3 9.1 1.0 SG A:CYS323 2.3 10.4 1.0 ND1 A:HIS349 2.4 8.3 1.0 CB A:CYS318 3.3 14.7 1.0 CB A:CYS323 3.3 7.4 1.0 CE1 A:HIS349 3.3 6.6 1.0 CB A:CYS320 3.4 7.6 1.0 CG A:HIS349 3.4 5.4 1.0 CB A:HIS349 3.7 4.9 1.0 N A:CYS323 3.9 9.6 1.0 N A:CYS320 4.1 13.1 1.0 CA A:HIS349 4.1 4.5 1.0 CA A:CYS320 4.2 11.1 1.0 CA A:CYS323 4.2 9.6 1.0 O A:CYS320 4.4 7.3 1.0 NE2 A:HIS349 4.5 6.4 1.0 O A:HIS349 4.5 9.5 1.0 CD2 A:HIS349 4.5 6.8 1.0 CA A:CYS318 4.6 15.4 1.0 C A:CYS320 4.6 9.8 1.0 C A:CYS318 4.6 17.0 1.0 CB A:VAL322 4.7 4.3 1.0 C A:HIS349 4.7 5.7 1.0 O A:CYS318 4.7 14.1 1.0 CB A:ALA352 4.9 7.9 1.0 C A:VAL322 4.9 7.9 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