Chlorine in PDB 4ce2: HSP90 N-Terminal Domain Bound to Macrolactam Analogues of Radicicol.

The structure of HSP90 N-Terminal Domain Bound to Macrolactam Analogues of Radicicol., PDB code: 4ce2 was solved by S.M.Roe, S.Parry-Morris, C.Prodromou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.46 / 2.38
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	74.320, 74.320, 110.460, 90.00, 90.00, 90.00
R / Rfree (%)	19.298 / 23.936

The binding sites of Chlorine atom in the HSP90 N-Terminal Domain Bound to Macrolactam Analogues of Radicicol. (pdb code 4ce2). 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 HSP90 N-Terminal Domain Bound to Macrolactam Analogues of Radicicol., PDB code: 4ce2:

Chlorine binding site 1 out of 1 in the HSP90 N-Terminal Domain Bound to Macrolactam Analogues of Radicicol.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of HSP90 N-Terminal Domain Bound to Macrolactam Analogues of Radicicol. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1215 b:63.5 occ:1.00 CL A:BO51215 0.0 63.5 1.0 C13 A:BO51215 1.7 54.3 1.0 C14 A:BO51215 2.6 45.3 1.0 C12 A:BO51215 2.7 56.9 1.0 O1 A:BO51215 2.8 43.2 1.0 C10 A:BO51215 2.9 61.4 1.0 C11 A:BO51215 2.9 58.4 1.0 CD1 A:PHE124 3.1 34.3 1.0 O A:BO51215 3.1 64.5 1.0 ND2 A:ASN37 3.3 34.5 1.0 C9 A:BO51215 3.6 62.5 1.0 CG A:PHE124 3.8 33.1 1.0 CE1 A:PHE124 3.9 37.7 1.0 CB A:PHE124 3.9 32.1 1.0 C15 A:BO51215 3.9 43.3 1.0 C17 A:BO51215 4.0 55.5 1.0 CB A:ASN37 4.1 29.9 1.0 CG A:ASN37 4.1 33.6 1.0 CD1 A:LEU173 4.4 36.9 1.0 CD2 A:LEU173 4.4 37.7 1.0 C16 A:BO51215 4.5 49.4 1.0 CA A:PHE124 4.8 29.3 1.0 CD2 A:LEU93 5.0 34.6 1.0 CG A:LEU173 5.0 34.2 1.0 CD2 A:PHE124 5.0 34.2 1.0

B.L.Dutton, R.R.A.Kitson, S.Parry-Morris, S.M.Roe, C.Prodromou, C.J.Moody. Synthesis of Macrolactam Analogues of Radicicol and Their Binding to Heat Shock Protein HSP90. Org.Biomol.Chem. 2014.
ISSN: ESSN 1477-0539
PubMed: 24435512
DOI: 10.1039/C3OB42211A