Chlorine in PDB 2fxs: Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radamide

The structure of Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radamide, PDB code: 2fxs was solved by R.M.Immormino, D.T.Gewirth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.41 / 2.00
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.205, 74.205, 110.852, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 22.6

The binding sites of Chlorine atom in the Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radamide (pdb code 2fxs). 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 Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radamide, PDB code: 2fxs:

Chlorine binding site 1 out of 1 in the Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radamide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1001 b:22.5 occ:1.00 CL A:RDA1001 0.0 22.5 1.0 C1 A:RDA1001 1.7 19.8 1.0 C2 A:RDA1001 2.7 18.9 1.0 C8 A:RDA1001 2.7 18.4 1.0 O1 A:RDA1001 2.9 17.4 1.0 C9 A:RDA1001 3.1 20.2 1.0 O A:HOH1221 3.3 54.2 1.0 CD1 A:PHE124 3.4 21.2 1.0 ND2 A:ASN37 3.5 25.9 1.0 C10 A:RDA1001 3.5 23.3 1.0 CG A:PHE124 3.9 20.4 1.0 CB A:PHE124 3.9 18.8 1.0 C3 A:RDA1001 4.0 18.3 1.0 C5 A:RDA1001 4.0 19.8 1.0 CG A:ASN37 4.1 22.7 1.0 CE1 A:PHE124 4.2 20.8 1.0 CB A:ASN37 4.2 20.9 1.0 CD2 A:LEU93 4.4 25.0 1.0 O5 A:RDA1001 4.4 29.0 1.0 C11 A:RDA1001 4.5 26.5 1.0 C4 A:RDA1001 4.5 17.6 1.0 O A:HOH1097 4.8 25.5 1.0 CA A:PHE124 4.8 17.3 1.0 CD2 A:PHE124 4.9 22.5 1.0

R.M.Immormino, L.E.Metzger, P.N.Reardon, D.E.Dollins, B.S.Blagg, D.T.Gewirth. Different Poses For Ligand and Chaperone in Inhibitor-Bound HSP90 and GRP94: Implications For Paralog-Specific Drug Design. J.Mol.Biol. V. 388 1033 2009.
ISSN: ISSN 0022-2836
PubMed: 19361515
DOI: 10.1016/J.JMB.2009.03.071