Fluorine 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:

Zinc	(Zn)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Fluorine 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 Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5, PDB code: 6ygw:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F 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:F95 b:14.2 occ:1.00 F A:FTR95 0.0 14.2 1.0 CZ3 A:FTR95 1.3 11.8 1.0 CH2 A:FTR95 2.3 10.9 1.0 CE3 A:FTR95 2.4 11.2 1.0 HH2 A:FTR95 2.5 13.1 1.0 HB2 A:ARG60 2.5 14.0 1.0 HE3 A:FTR95 2.6 13.4 1.0 HG12 A:VAL59 2.6 14.2 1.0 HB A:VAL59 2.7 13.2 1.0 H A:ARG60 2.8 12.3 1.0 N A:ARG60 2.8 10.3 1.0 HA A:ARG60 2.9 12.8 1.0 CA A:ARG60 3.1 10.7 1.0 O A:PRO56 3.1 11.2 1.0 CB A:ARG60 3.2 11.7 1.0 CG1 A:VAL59 3.3 11.9 1.0 CB A:VAL59 3.3 11.0 1.0 C A:VAL59 3.4 10.5 1.0 HG11 A:VAL59 3.6 14.2 1.0 CZ2 A:FTR95 3.6 10.2 1.0 CD2 A:FTR95 3.6 10.0 1.0 HB3 A:ARG60 3.8 14.0 1.0 HB3 A:ALA64 3.9 13.4 1.0 HD3 A:ARG60 3.9 14.0 1.0 CA A:VAL59 3.9 10.4 1.0 O A:VAL59 4.0 10.9 1.0 CE2 A:FTR95 4.0 10.0 1.0 HG13 A:VAL59 4.1 14.2 1.0 C A:PRO56 4.2 11.0 1.0 HA A:PRO56 4.2 13.7 1.0 C3 A:GOL402 4.3 22.7 1.0 HD2 A:ARG60 4.3 14.0 1.0 HZ2 A:FTR95 4.3 12.3 1.0 O A:ALA64 4.3 10.5 1.0 CG A:ARG60 4.3 11.9 1.0 CD A:ARG60 4.4 11.7 1.0 C1 A:GOL402 4.4 23.5 1.0 HD2 A:ARG97 4.5 16.1 1.0 HG23 A:ILE67 4.5 12.5 1.0 HB3 A:PRO56 4.5 15.8 1.0 N A:VAL59 4.6 10.5 1.0 C A:ARG60 4.6 11.4 1.0 CA A:PRO56 4.7 11.4 1.0 H A:VAL59 4.7 12.7 1.0 CG2 A:VAL59 4.7 11.8 1.0 HA A:VAL59 4.7 12.5 1.0 HG2 A:ARG60 4.7 14.3 1.0 HG21 A:VAL59 4.7 14.1 1.0 CB A:ALA64 4.8 11.1 1.0 HG21 A:ILE67 4.8 12.5 1.0 CG A:FTR95 5.0 10.2 1.0 HB1 A:ALA64 5.0 13.4 1.0 HG23 A:VAL59 5.0 14.1 1.0

Fluorine binding site 2 out of 3 in the Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 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:F296 b:24.1 occ:1.00 F A:FTR296 0.0 24.1 1.0 CZ3 A:FTR296 1.3 21.5 1.0 CH2 A:FTR296 2.3 21.6 1.0 CE3 A:FTR296 2.4 18.6 1.0 HH2 A:FTR296 2.5 25.9 1.0 HD13 A:LEU357 2.5 16.9 1.0 HE3 A:FTR296 2.6 22.3 1.0 HD1 A:PHE377 2.8 20.5 1.0 HE1 A:PHE377 2.9 21.8 1.0 HD12 A:LEU357 3.1 16.9 1.0 HZ A:PHE373 3.1 20.4 1.0 CD1 A:LEU357 3.2 14.1 1.0 HD2 A:LYS360 3.3 23.5 1.0 CD1 A:PHE377 3.3 17.1 1.0 HA A:LEU357 3.3 12.8 1.0 CE1 A:PHE377 3.4 18.2 1.0 HB2 A:LEU357 3.5 14.1 1.0 CD2 A:FTR296 3.6 16.8 1.0 CZ2 A:FTR296 3.6 20.4 1.0 HD11 A:LEU357 3.9 16.9 1.0 CZ A:PHE373 4.0 17.0 1.0 CB A:LEU357 4.0 11.8 1.0 HZ A:PHE353 4.0 21.1 1.0 CE2 A:FTR296 4.1 18.1 1.0 CD A:LYS360 4.1 19.6 1.0 CA A:LEU357 4.1 10.7 1.0 HD3 A:LYS360 4.1 23.5 1.0 HE3 A:LYS360 4.2 27.0 1.0 CG A:LEU357 4.2 12.5 1.0 HE1 A:PHE373 4.2 20.8 1.0 HZ2 A:FTR296 4.3 24.5 1.0 CZ A:PHE353 4.4 17.6 1.0 C1 A:GOL401 4.5 34.5 1.0 CG A:PHE377 4.5 15.6 1.0 CE1 A:PHE373 4.6 17.3 1.0 HB2 A:LYS360 4.6 16.0 1.0 HD22 A:LEU357 4.6 17.2 1.0 HB2 A:PHE377 4.6 18.5 1.0 CZ A:PHE377 4.6 18.4 1.0 CE A:LYS360 4.7 22.5 1.0 N A:LEU357 4.8 10.7 1.0 O A:HOH579 4.8 16.3 1.0 HE1 A:PHE353 4.9 21.2 1.0 HA A:FTR296 4.9 16.8 1.0 CE1 A:PHE353 4.9 17.6 1.0 HG A:LEU357 4.9 15.0 1.0 CG A:FTR296 4.9 14.7 1.0 HB3 A:LEU357 4.9 14.1 1.0 CD2 A:LEU357 5.0 14.3 1.0 CE2 A:PHE353 5.0 16.2 1.0 HZ A:PHE377 5.0 22.1 1.0

Fluorine binding site 3 out of 3 in the Tgt W178F Mutant Labelled Mit 5F-Trp Crystallised at pH 5.5


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 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:F326 b:13.6 occ:1.00 F A:FTR326 0.0 13.6 1.0 CZ3 A:FTR326 1.3 11.8 1.0 CH2 A:FTR326 2.4 11.9 1.0 CE3 A:FTR326 2.4 11.0 1.0 HH2 A:FTR326 2.5 14.2 1.0 HE3 A:FTR326 2.6 13.2 1.0 HA A:VAL322 2.6 12.7 1.0 HD22 A:LEU345 2.9 13.6 1.0 HG22 A:VAL322 3.0 13.2 1.0 HD2 A:LYS325 3.1 25.8 1.0 HD21 A:LEU345 3.3 13.6 1.0 HB2 A:LYS325 3.4 18.9 1.0 CA A:VAL322 3.5 10.6 1.0 CD2 A:LEU345 3.5 11.3 1.0 O A:ALA321 3.6 12.6 1.0 CD2 A:FTR326 3.6 10.7 1.0 CZ2 A:FTR326 3.6 11.9 1.0 N A:VAL322 3.7 10.8 1.0 C A:ALA321 3.8 11.5 1.0 CG2 A:VAL322 3.9 11.0 1.0 HD23 A:LEU345 3.9 13.6 1.0 O A:HOH901 3.9 20.1 1.0 HB1 A:ALA321 3.9 16.0 1.0 CD A:LYS325 4.0 21.5 1.0 HG13 A:VAL322 4.0 13.2 1.0 CE2 A:FTR326 4.1 11.1 1.0 HB3 A:ALA321 4.1 16.0 1.0 HG23 A:VAL322 4.1 13.2 1.0 CB A:VAL322 4.2 10.7 1.0 H A:VAL322 4.2 13.0 1.0 HD3 A:LYS325 4.2 25.8 1.0 CB A:LYS325 4.3 15.7 1.0 HZ2 A:FTR326 4.4 14.3 1.0 CB A:ALA321 4.4 13.4 1.0 HD13 A:LEU345 4.5 13.4 1.0 C A:VAL322 4.6 11.0 1.0 HB3 A:LYS325 4.6 18.9 1.0 HG21 A:VAL322 4.6 13.2 1.0 CG1 A:VAL322 4.6 11.0 1.0 CG A:LYS325 4.6 19.0 1.0 O A:VAL322 4.7 12.1 1.0 OE1 A:GLU348 4.7 11.2 1.0 CA A:ALA321 4.7 12.2 1.0 HG3 A:LYS325 4.8 22.8 1.0 CG A:LEU345 4.8 10.9 1.0 HD11 A:LEU345 4.9 13.4 1.0 CG A:FTR326 4.9 10.9 1.0 CD1 A:LEU345 5.0 11.2 1.0 CE A:LYS325 5.0 23.4 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.