Chlorine in PDB 4egk: Human HSP90-Alpha Atpase Domain Bound to Radicicol

The structure of Human HSP90-Alpha Atpase Domain Bound to Radicicol, PDB code: 4egk was solved by W.J.Chen, S.P.Wood, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.71 / 1.69
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.440, 43.880, 53.640, 90.00, 113.81, 90.00
R / Rfree (%)	20.1 / 24.3

The binding sites of Chlorine atom in the Human HSP90-Alpha Atpase Domain Bound to Radicicol (pdb code 4egk). 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 Human HSP90-Alpha Atpase Domain Bound to Radicicol, PDB code: 4egk:

Chlorine binding site 1 out of 1 in the Human HSP90-Alpha Atpase Domain Bound to Radicicol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human HSP90-Alpha Atpase Domain Bound to Radicicol within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:10.7 occ:1.00 CL1 A:RDC301 0.0 10.7 1.0 C6 A:RDC301 1.7 10.3 1.0 C5 A:RDC301 2.7 10.5 1.0 C7 A:RDC301 2.8 11.4 1.0 O4 A:RDC301 2.9 11.2 1.0 C9 A:RDC301 3.0 13.5 1.0 C8 A:RDC301 3.0 11.5 1.0 O5 A:RDC301 3.2 13.9 1.0 CD1 A:PHE138 3.4 11.3 1.0 ND2 A:ASN51 3.4 12.1 1.0 C10 A:RDC301 3.8 13.4 1.0 CB A:PHE138 4.0 9.8 1.0 CG A:PHE138 4.0 10.3 1.0 C4 A:RDC301 4.0 10.1 1.0 C2 A:RDC301 4.1 10.2 1.0 CE1 A:PHE138 4.2 11.5 1.0 CD2 A:LEU107 4.3 12.2 1.0 CG A:ASN51 4.4 12.3 1.0 C11 A:RDC301 4.4 12.8 1.0 CB A:ASN51 4.4 10.7 1.0 C3 A:RDC301 4.5 11.3 1.0 CD2 A:LEU48 4.7 10.7 1.0 CD1 A:LEU107 4.8 11.9 1.0 CG2 A:VAL186 4.8 10.6 1.0 O A:HOH462 4.8 18.4 1.0 CA A:PHE138 4.9 9.1 1.0 CG A:LEU107 5.0 11.9 1.0

C.Austin, S.N.Pettit, S.K.Magnolo, J.Sanvoisin, W.Chen, S.P.Wood, L.D.Freeman, R.J.Pengelly, D.E.Hughes. Fragment Screening Using Capillary Electrophoresis (Cefrag) For Hit Identification of Heat Shock Protein 90 Atpase Inhibitors. J Biomol Screen V. 17 868 2012.
ISSN: ISSN 1087-0571
PubMed: 22573733
DOI: 10.1177/1087057112445785