Fluorine in PDB 2qfo: HSP90 Complexed with A143571 and A516383

The structure of HSP90 Complexed with A143571 and A516383, PDB code: 2qfo was solved by C.H.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.68
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	64.157, 88.755, 98.445, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Fluorine atom in the HSP90 Complexed with A143571 and A516383 (pdb code 2qfo). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the HSP90 Complexed with A143571 and A516383, PDB code: 2qfo:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the HSP90 Complexed with A143571 and A516383


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of HSP90 Complexed with A143571 and A516383 within 5.0Å range: probe atom residue distance (Å) B Occ A:F900 b:17.8 occ:1.00 F10 A:A13900 0.0 17.8 1.0 C9 A:A13900 1.3 16.6 1.0 F12 A:A13900 2.2 17.6 1.0 F11 A:A13900 2.2 17.4 1.0 C3 A:A13900 2.3 16.1 1.0 N4 A:A13900 2.9 15.4 1.0 C2 A:A13900 3.4 15.6 1.0 O A:HOH1002 3.5 10.5 1.0 CD2 A:LEU107 3.5 13.3 1.0 CE A:MET98 3.7 11.2 1.0 CD1 A:PHE138 3.8 9.2 1.0 C5 A:A13900 4.1 14.7 1.0 CG A:LEU107 4.2 13.2 1.0 CG A:PHE138 4.2 9.3 1.0 CE1 A:PHE138 4.2 9.9 1.0 CD1 A:LEU107 4.3 13.3 1.0 SD A:MET98 4.3 11.5 1.0 CB A:PHE138 4.6 8.8 1.0 C1 A:A13900 4.6 15.3 1.0 N6 A:A13900 4.9 15.2 1.0 ND2 A:ASN51 5.0 11.4 1.0 N7 A:A13900 5.0 14.1 1.0

Fluorine binding site 2 out of 3 in the HSP90 Complexed with A143571 and A516383


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of HSP90 Complexed with A143571 and A516383 within 5.0Å range: probe atom residue distance (Å) B Occ A:F900 b:17.4 occ:1.00 F11 A:A13900 0.0 17.4 1.0 C9 A:A13900 1.3 16.6 1.0 F10 A:A13900 2.2 17.8 1.0 F12 A:A13900 2.2 17.6 1.0 C3 A:A13900 2.3 16.1 1.0 N4 A:A13900 2.8 15.4 1.0 C7 A:A51999 3.1 17.4 1.0 O A:HOH1002 3.1 10.5 1.0 ND2 A:ASN51 3.2 11.4 1.0 C3 A:A51999 3.5 16.3 1.0 C2 A:A13900 3.5 15.6 1.0 N8 A:A51999 3.6 17.8 1.0 CG A:ASN51 3.7 10.5 1.0 C10 A:A51999 3.7 18.9 1.0 C4 A:A51999 3.9 15.9 1.0 C9 A:A51999 3.9 18.7 1.0 CB A:PHE138 3.9 8.8 1.0 O6 A:A51999 4.0 14.5 1.0 C5 A:A13900 4.1 14.7 1.0 CB A:ASN51 4.1 9.4 1.0 C2 A:A51999 4.3 16.5 1.0 CD1 A:PHE138 4.3 9.2 1.0 OD1 A:ASN51 4.4 11.4 1.0 CG A:PHE138 4.4 9.3 1.0 CD2 A:LEU107 4.5 13.3 1.0 C11 A:A51999 4.7 18.7 1.0 C1 A:A13900 4.7 15.3 1.0 O5 A:A51999 4.7 15.9 1.0 N6 A:A13900 4.9 15.2 1.0 N7 A:A13900 4.9 14.1 1.0 C14 A:A51999 5.0 18.6 1.0 CA A:PHE138 5.0 8.8 1.0

Fluorine binding site 3 out of 3 in the HSP90 Complexed with A143571 and A516383


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of HSP90 Complexed with A143571 and A516383 within 5.0Å range: probe atom residue distance (Å) B Occ A:F900 b:17.6 occ:1.00 F12 A:A13900 0.0 17.6 1.0 C9 A:A13900 1.3 16.6 1.0 F10 A:A13900 2.2 17.8 1.0 F11 A:A13900 2.2 17.4 1.0 C3 A:A13900 2.3 16.1 1.0 C2 A:A13900 2.7 15.6 1.0 N8 A:A51999 3.5 17.8 1.0 N4 A:A13900 3.6 15.4 1.0 C7 A:A51999 3.7 17.4 1.0 SD A:MET98 3.7 11.5 1.0 CD2 A:LEU107 3.8 13.3 1.0 C9 A:A51999 3.8 18.7 1.0 ND2 A:ASN106 3.9 16.1 1.0 CB A:ASN106 3.9 15.4 1.0 C3 A:A51999 3.9 16.3 1.0 CE A:MET98 4.1 11.2 1.0 C2 A:A51999 4.1 16.5 1.0 C1 A:A13900 4.2 15.3 1.0 C10 A:A51999 4.3 18.9 1.0 CG A:ASN106 4.3 16.3 1.0 C14 A:A51999 4.3 18.6 1.0 CG A:LEU107 4.5 13.2 1.0 C5 A:A13900 4.6 14.7 1.0 O A:HOH1110 4.8 30.8 1.0 C4 A:A51999 4.8 15.9 1.0 O A:HOH1002 4.9 10.5 1.0 CG A:MET98 5.0 11.2 1.0 N6 A:A13900 5.0 15.2 1.0

J.R.Huth, C.Park, A.M.Petros, A.R.Kunzer, M.D.Wendt, X.Wang, C.L.Lynch, J.C.Mack, K.M.Swift, R.A.Judge, J.Chen, P.L.Richardson, S.Jin, S.K.Tahir, E.D.Matayoshi, S.A.Dorwin, U.S.Ladror, J.M.Severin, K.A.Walter, D.M.Bartley, S.W.Fesik, S.W.Elmore, P.J.Hajduk. Discovery and Design of Novel HSP90 Inhibitors Using Multiple Fragment-Based Design Strategies. Chem.Biol.Drug Des. V. 70 1 2007.
ISSN: ISSN 1747-0277
PubMed: 17630989
DOI: 10.1111/J.1747-0285.2007.00535.X