Zinc in PDB 6yfw: Tgt H333F Mutant Crystallised at pH 8.5

All present enzymatic activity of Tgt H333F Mutant Crystallised at pH 8.5:
2.4.2.29;

The structure of Tgt H333F Mutant Crystallised at pH 8.5, PDB code: 6yfw 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)	43.41 / 1.26
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.596, 64.971, 70.507, 90.00, 95.92, 90.00
R / Rfree (%)	13 / 15.4

The structure of Tgt H333F Mutant Crystallised at pH 8.5 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Zinc atom in the Tgt H333F Mutant Crystallised at pH 8.5 (pdb code 6yfw). 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 Tgt H333F Mutant Crystallised at pH 8.5, PDB code: 6yfw:

Zinc binding site 1 out of 1 in the Tgt H333F Mutant Crystallised at pH 8.5


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Tgt H333F Mutant Crystallised at pH 8.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:12.5 occ:1.00 ND1 A:HIS349 2.1 11.7 1.0 SG A:CYS320 2.3 12.8 1.0 SG A:CYS323 2.3 13.0 1.0 SG A:CYS318 2.3 13.9 1.0 CE1 A:HIS349 2.9 12.2 1.0 HE1 A:HIS349 3.0 14.7 1.0 HB2 A:CYS323 3.0 14.9 1.0 HB3 A:CYS318 3.0 17.5 1.0 HB3 A:CYS320 3.2 15.1 1.0 CG A:HIS349 3.3 10.9 1.0 CB A:CYS318 3.3 14.6 1.0 CB A:CYS323 3.3 12.4 1.0 H A:CYS323 3.3 14.9 1.0 HB2 A:HIS349 3.3 13.4 1.0 CB A:CYS320 3.4 12.6 1.0 H A:CYS320 3.5 16.5 1.0 HA A:HIS349 3.5 13.4 1.0 HB2 A:CYS318 3.7 17.5 1.0 CB A:HIS349 3.7 11.2 1.0 HB A:VAL322 3.8 14.3 1.0 N A:CYS323 3.9 12.4 1.0 HB3 A:CYS323 4.0 14.9 1.0 CA A:HIS349 4.1 11.1 1.0 N A:CYS320 4.1 13.8 1.0 NE2 A:HIS349 4.1 12.9 1.0 HB2 A:CYS320 4.1 15.1 1.0 CA A:CYS320 4.2 13.1 1.0 CA A:CYS323 4.2 12.3 1.0 HB2 A:LEU314 4.2 15.2 1.0 CD2 A:HIS349 4.3 12.1 1.0 HB3 A:ASP315 4.4 19.1 1.0 HB3 A:ALA352 4.5 15.0 1.0 O A:HIS349 4.5 11.1 1.0 HE22 A:GLN356 4.5 20.0 1.0 HD12 A:LEU314 4.6 16.2 1.0 CA A:CYS318 4.6 15.0 1.0 H A:ASP315 4.6 16.9 1.0 HA A:CYS323 4.6 14.8 1.0 HB3 A:HIS349 4.6 13.4 1.0 C A:CYS318 4.7 15.3 1.0 O A:CYS320 4.7 14.0 1.0 C A:CYS320 4.7 12.9 1.0 O A:CYS318 4.7 16.2 1.0 H A:VAL322 4.8 15.6 1.0 C A:HIS349 4.8 11.2 1.0 CB A:VAL322 4.8 11.9 1.0 HE2 A:HIS349 4.9 15.6 1.0 C A:VAL322 4.9 12.8 1.0

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