Zinc in PDB 4htb: Trna-Guanine Transglycosylase Y330C Mutant in Space Group C2

All present enzymatic activity of Trna-Guanine Transglycosylase Y330C Mutant in Space Group C2:
2.4.2.29;

The structure of Trna-Guanine Transglycosylase Y330C Mutant in Space Group C2, PDB code: 4htb was solved by S.Jakobi, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.14 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.968, 64.660, 70.563, 90.00, 95.53, 90.00
R / Rfree (%)	18 / 21.4

The binding sites of Zinc atom in the Trna-Guanine Transglycosylase Y330C Mutant in Space Group C2 (pdb code 4htb). 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 Y330C Mutant in Space Group C2, PDB code: 4htb:

Zinc binding site 1 out of 1 in the Trna-Guanine Transglycosylase Y330C Mutant in Space Group C2


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 Y330C Mutant in Space Group C2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:20.9 occ:1.00 ND1 A:HIS349 2.1 17.1 1.0 SG A:CYS318 2.3 23.0 1.0 SG A:CYS320 2.3 22.6 1.0 SG A:CYS323 2.4 21.0 1.0 CE1 A:HIS349 2.9 22.7 1.0 CG A:HIS349 3.2 18.4 1.0 CB A:CYS318 3.3 20.8 1.0 CB A:CYS323 3.3 22.0 1.0 CB A:CYS320 3.3 17.5 1.0 CB A:HIS349 3.7 19.9 1.0 N A:CYS323 3.9 20.7 1.0 CA A:HIS349 4.1 19.1 1.0 NE2 A:HIS349 4.1 20.7 1.0 N A:CYS320 4.1 17.0 1.0 CA A:CYS320 4.2 21.3 1.0 CA A:CYS323 4.2 22.4 1.0 CD2 A:HIS349 4.3 19.8 1.0 O A:HIS349 4.5 18.8 1.0 CA A:CYS318 4.6 25.4 1.0 O A:CYS320 4.6 22.9 1.0 C A:CYS320 4.6 23.6 1.0 C A:CYS318 4.7 28.5 1.0 C A:HIS349 4.7 18.4 1.0 CB A:VAL322 4.8 21.7 1.0 O A:CYS318 4.9 27.5 1.0 C A:VAL322 5.0 22.5 1.0

S.Jakobi, G.Klebe. Y330C Mutant of Trna-Guanin Transglycosylase Results in Covalently Bound Dimer in Novel Interface Conformation and New Crystal Packing To Be Published.