Fluorine in PDB 6h8s: Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314

All present enzymatic activity of Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314:
3.1.3.48;

The structure of Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314, PDB code: 6h8s was solved by D.Fiegen, G.Schnapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.19 / 1.77
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.303, 59.303, 181.641, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 21.2

The binding sites of Fluorine atom in the Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314 (pdb code 6h8s). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314, PDB code: 6h8s:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:31.5 occ:0.76 F15 A:FSZ601 0.0 31.5 0.8 C14 A:FSZ601 1.3 27.2 0.8 F16 A:FSZ601 2.1 29.7 0.8 F17 A:FSZ601 2.1 24.4 0.8 C12 A:FSZ601 2.4 22.3 0.8 C11 A:FSZ601 2.8 22.6 0.8 OG A:SER486 3.1 20.0 0.8 O A:HOH750 3.1 26.6 1.0 CG A:GLU455 3.3 26.5 1.0 OE1 A:GLN490 3.4 27.6 1.0 C13 A:FSZ601 3.6 19.2 0.8 O A:HOH704 3.6 29.8 1.0 CB A:GLU455 3.8 15.0 1.0 CA A:GLU455 3.9 13.4 1.0 OH A:TYR345 3.9 23.2 1.0 CD A:GLN490 4.1 34.2 1.0 C10 A:FSZ601 4.2 23.1 0.8 CD A:GLU455 4.3 37.5 1.0 CB A:SER486 4.4 13.3 0.2 CB A:SER486 4.4 13.2 0.8 O A:SER486 4.5 15.6 0.2 N A:GLU455 4.6 12.9 1.0 O A:SER486 4.6 16.6 0.8 NE2 A:GLN490 4.7 19.0 1.0 C8 A:FSZ601 4.7 18.4 0.8 OE2 A:GLU455 4.8 18.4 1.0 O A:HOH838 4.8 18.6 1.0 CZ A:TYR345 4.8 21.0 1.0 C5 A:FSZ601 4.9 29.7 0.8 CG A:GLN490 4.9 24.4 1.0 CE2 A:TYR345 4.9 16.6 1.0 CB A:ALA458 4.9 18.2 1.0 C9 A:FSZ601 5.0 20.2 0.8 C A:SER486 5.0 15.3 0.2 OE1 A:GLU455 5.0 30.4 1.0 C A:SER486 5.0 15.8 0.8 OG A:SER486 5.0 19.9 0.2

Fluorine binding site 2 out of 3 in the Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:29.7 occ:0.76 F16 A:FSZ601 0.0 29.7 0.8 C14 A:FSZ601 1.3 27.2 0.8 F17 A:FSZ601 2.1 24.4 0.8 F15 A:FSZ601 2.1 31.5 0.8 C12 A:FSZ601 2.4 22.3 0.8 C13 A:FSZ601 2.8 19.2 0.8 OH A:TYR345 2.9 23.2 1.0 CE2 A:TYR345 3.1 16.6 1.0 OG A:SER486 3.1 20.0 0.8 CZ A:TYR345 3.3 21.0 1.0 C11 A:FSZ601 3.6 22.6 0.8 CD1 A:ILE468 3.7 17.3 1.0 O A:HOH750 3.8 26.6 1.0 C8 A:FSZ601 4.2 18.4 0.8 CD2 A:TYR345 4.2 15.2 1.0 CG1 A:VAL344 4.3 14.7 1.0 O A:HOH838 4.4 18.6 1.0 CB A:SER486 4.5 13.3 0.2 CB A:SER486 4.5 13.2 0.8 OE1 A:GLN490 4.5 27.6 1.0 CE1 A:TYR345 4.5 16.0 1.0 C10 A:FSZ601 4.8 23.1 0.8 OG A:SER486 4.9 19.9 0.2 CB A:ALA458 4.9 18.2 1.0 C9 A:FSZ601 5.0 20.2 0.8

Fluorine binding site 3 out of 3 in the Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of the Mouse Protein Tyrosine Phosphatase PTPN5 (Step) in Complex with Compound Bi-0314 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:24.4 occ:0.76 F17 A:FSZ601 0.0 24.4 0.8 C14 A:FSZ601 1.3 27.2 0.8 F16 A:FSZ601 2.1 29.7 0.8 F15 A:FSZ601 2.1 31.5 0.8 C12 A:FSZ601 2.4 22.3 0.8 C11 A:FSZ601 3.2 22.6 0.8 C13 A:FSZ601 3.2 19.2 0.8 O A:HOH750 3.3 26.6 1.0 CB A:ALA458 3.3 18.2 1.0 CA A:GLU455 3.4 13.4 1.0 CD1 A:ILE468 3.4 17.3 1.0 O A:VAL454 3.7 14.8 1.0 N A:GLU455 3.8 12.9 1.0 CG1 A:VAL454 3.9 14.6 1.0 C A:VAL454 3.9 15.6 1.0 CB A:GLU455 4.1 15.0 1.0 OG A:SER486 4.2 20.0 0.8 CG A:GLU455 4.2 26.5 1.0 C10 A:FSZ601 4.4 23.1 0.8 C8 A:FSZ601 4.4 18.4 0.8 C A:GLU455 4.5 16.9 1.0 O A:GLU455 4.5 15.9 1.0 CA A:ALA458 4.7 18.3 1.0 CB A:VAL454 4.8 14.5 1.0 CE2 A:TYR345 4.9 16.6 1.0 OH A:TYR345 4.9 23.2 1.0 C9 A:FSZ601 4.9 20.2 0.8 N A:ALA458 5.0 17.6 1.0 CA A:VAL454 5.0 11.8 1.0

C.S.Tautermann, F.Binder, F.H.Buttner, C.Eickmeier, D.Fiegen, U.Gross, M.A.Grundl, R.Heilker, S.Hobson, S.Hoerer, A.Luippold, V.Mack, F.Montel, S.Peters, S.Bhattacharya, N.Vaidehi, G.Schnapp, S.Thamm, M.Zeeb. Allosteric Activation of Striatal-Enriched Protein Tyrosine Phosphatase (Step, PTPN5) By A Fragment-Like Molecule. J. Med. Chem. V. 62 306 2019.
ISSN: ISSN 1520-4804
PubMed: 30207464
DOI: 10.1021/ACS.JMEDCHEM.8B00857