Chlorine in PDB 6ygw: Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5

All present enzymatic activity of Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5:
2.4.2.29;

The structure of Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5, PDB code: 6ygw 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)	44.91 / 1.16
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.305, 65.345, 70.134, 90.00, 95.99, 90.00
R / Rfree (%)	11.4 / 13.2

The structure of Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5 also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Zinc	(Zn)	1 atom

The binding sites of Chlorine atom in the Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5 (pdb code 6ygw). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5, PDB code: 6ygw:

Chlorine binding site 1 out of 1 in the Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:17.7 occ:1.00 HH12 A:ARG289 2.4 18.1 1.0 HG1 A:THR285 2.7 15.4 1.0 O A:HOH591 2.7 40.0 1.0 HD2 A:LYS52 3.0 20.6 1.0 OG1 A:THR285 3.0 12.8 1.0 HB A:THR285 3.1 15.6 1.0 HH22 A:ARG289 3.2 21.5 1.0 HB A:VAL282 3.2 17.2 1.0 O A:HOH559 3.2 21.4 1.0 NH1 A:ARG289 3.2 15.1 1.0 HB2 A:ARG286 3.3 18.6 0.6 HB2 A:ARG286 3.3 19.4 0.4 CB A:THR285 3.5 13.0 1.0 H A:ARG286 3.6 16.4 0.4 H A:ARG286 3.6 16.1 0.6 HG12 A:VAL282 3.8 18.5 1.0 HH11 A:ARG289 3.8 18.1 1.0 HG1 A:THR47 3.8 34.0 1.0 N A:ARG286 3.8 13.7 0.4 N A:ARG286 3.8 13.4 0.6 CD A:LYS52 3.9 17.2 1.0 NH2 A:ARG289 3.9 17.9 1.0 HB2 A:LYS52 3.9 14.8 1.0 HE3 A:LYS52 4.0 25.3 1.0 HA A:ARG286 4.0 16.8 0.6 CZ A:ARG289 4.0 16.5 1.0 HE A:ARG286 4.0 27.8 0.6 HA A:ARG286 4.0 17.4 0.4 HE2 A:LYS52 4.0 25.3 1.0 CB A:VAL282 4.0 14.3 1.0 HG11 A:VAL282 4.1 18.5 1.0 HG3 A:LYS52 4.1 16.8 1.0 CB A:ARG286 4.1 15.5 0.6 CB A:ARG286 4.1 16.2 0.4 CG1 A:VAL282 4.2 15.4 1.0 CE A:LYS52 4.2 21.1 1.0 CA A:ARG286 4.2 14.0 0.6 CA A:ARG286 4.2 14.5 0.4 OG1 A:THR47 4.3 28.3 1.0 HA A:VAL282 4.3 14.8 1.0 C A:THR285 4.3 12.9 1.0 O A:VAL282 4.4 12.9 1.0 CG A:LYS52 4.4 14.0 1.0 HG21 A:THR285 4.5 17.1 1.0 CA A:THR285 4.5 12.8 1.0 HD3 A:LYS52 4.6 20.6 1.0 HH21 A:ARG286 4.6 31.2 0.6 CG2 A:THR285 4.6 14.2 1.0 HH21 A:ARG289 4.6 21.5 1.0 HB3 A:ARG286 4.7 19.4 0.4 CB A:LYS52 4.7 12.3 1.0 HB A:VAL45 4.7 14.4 1.0 H A:LYS52 4.7 13.1 1.0 HB3 A:ARG286 4.7 18.6 0.6 CA A:VAL282 4.7 12.3 1.0 HD3 A:ARG286 4.8 24.1 0.4 NE A:ARG286 4.8 23.2 0.6 HG3 A:ARG286 4.9 21.3 0.6 O A:HOH655 4.9 14.2 1.0 O A:VAL45 5.0 12.8 1.0 HG12 A:VAL45 5.0 16.1 1.0

A.Nguyen, A.Heine, G.Klebe. Mutation Study on Trna-Guanine Transglycosylase Within 19F uc(Nmr) Experiments For Conformational Change Analysis To Be Published.