Fluorine in PDB 4hy6: Crystal Structure of the Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1

The structure of Crystal Structure of the Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1, PDB code: 4hy6 was solved by M.Yang, J.Li, J.H.He, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.53 / 1.65
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.061, 91.034, 99.177, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 21.6

The binding sites of Fluorine atom in the Crystal Structure of the Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1 (pdb code 4hy6). 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 Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1, PDB code: 4hy6:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of the Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1


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 Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:27.2 occ:1.00 F14 A:FJ1501 0.0 27.2 1.0 C13 A:FJ1501 1.3 26.0 1.0 F16 A:FJ1501 2.2 31.7 1.0 F15 A:FJ1501 2.2 29.9 1.0 C09 A:FJ1501 2.3 20.3 1.0 C05 A:FJ1501 3.2 20.3 1.0 N08 A:FJ1501 3.3 21.7 1.0 O12 A:FJ1501 3.4 24.6 1.0 CE2 A:TYR139 3.4 20.2 1.0 C04 A:FJ1501 3.7 21.3 1.0 CD2 A:TYR139 3.7 16.9 1.0 O A:HOH624 3.8 19.2 1.0 CA A:VAL136 3.8 17.8 1.0 CB A:ALA111 3.9 29.9 1.0 O A:GLY135 3.9 21.3 1.0 CG1 A:VAL136 4.0 21.1 1.0 CB A:VAL136 4.1 17.7 1.0 C06 A:FJ1501 4.3 20.0 1.0 CB A:PHE138 4.3 15.2 1.0 N07 A:FJ1501 4.3 22.1 1.0 C A:VAL136 4.4 16.5 1.0 O A:VAL136 4.6 16.8 1.0 CZ A:TYR139 4.6 19.5 1.0 C A:GLY135 4.8 19.2 1.0 N A:VAL136 4.8 19.2 1.0 CD2 A:PHE138 5.0 16.1 1.0 N A:PHE138 5.0 15.0 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of the Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1


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 Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:29.9 occ:1.00 F15 A:FJ1501 0.0 29.9 1.0 C13 A:FJ1501 1.3 26.0 1.0 F16 A:FJ1501 2.2 31.7 1.0 F14 A:FJ1501 2.2 27.2 1.0 C09 A:FJ1501 2.3 20.3 1.0 O12 A:FJ1501 3.0 24.6 1.0 O A:LEU107 3.0 25.0 1.0 C05 A:FJ1501 3.1 20.3 1.0 CB A:ALA111 3.4 29.9 1.0 N08 A:FJ1501 3.4 21.7 1.0 C04 A:FJ1501 3.5 21.3 1.0 C A:LEU107 3.6 21.4 1.0 CB A:LEU107 3.7 22.4 1.0 CA A:LEU107 4.1 21.9 1.0 C06 A:FJ1501 4.3 20.0 1.0 N A:GLY108 4.4 21.9 1.0 N07 A:FJ1501 4.4 22.1 1.0 CA A:ALA111 4.4 30.0 1.0 N A:ALA111 4.6 28.9 1.0 O A:GLY135 4.7 21.3 1.0 CG A:LEU107 4.7 24.6 1.0 CA A:GLY108 4.8 24.4 1.0 CE2 A:TYR139 4.8 20.2 1.0 CD2 A:LEU107 4.9 28.4 1.0 C01 A:FJ1501 4.9 18.2 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of the Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1


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 Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:31.7 occ:1.00 F16 A:FJ1501 0.0 31.7 1.0 C13 A:FJ1501 1.3 26.0 1.0 F14 A:FJ1501 2.2 27.2 1.0 F15 A:FJ1501 2.2 29.9 1.0 C09 A:FJ1501 2.3 20.3 1.0 N08 A:FJ1501 2.6 21.7 1.0 O A:GLY135 2.9 21.3 1.0 O A:HOH624 3.2 19.2 1.0 C05 A:FJ1501 3.7 20.3 1.0 N07 A:FJ1501 3.9 22.1 1.0 C A:GLY135 4.1 19.2 1.0 CA A:VAL136 4.3 17.8 1.0 C06 A:FJ1501 4.5 20.0 1.0 CB A:ALA111 4.6 29.9 1.0 N A:VAL136 4.7 19.2 1.0 O12 A:FJ1501 4.7 24.6 1.0 C04 A:FJ1501 4.7 21.3 1.0 CG1 A:VAL136 4.8 21.1 1.0 O A:LEU107 4.8 25.0 1.0

M.Yang, J.Li, J.H.He. Crystal Structure of the Human HSP90-Alpha N-Domain Bound to the HSP90 Inhibitor FJ1 To Be Published.