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Chlorine in PDB 1zwh: Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radester Amine

Protein crystallography data

The structure of Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radester Amine, PDB code: 1zwh was solved by R.M.Immormino, B.S.Blagg, D.T.Gewirth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.24 / 1.65
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.884, 73.884, 110.621, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 20.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radester Amine (pdb code 1zwh). 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 Radester Amine, PDB code: 1zwh:

Chlorine binding site 1 out of 1 in 1zwh

Go back to Chlorine Binding Sites List in 1zwh
Chlorine binding site 1 out of 1 in the Yeast HSP82 in Complex with the Novel HSP90 Inhibitor Radester Amine


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 Radester Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1001

b:31.6
occ:1.00
CLAH A:RDE1001 0.0 31.6 1.0
CAV A:RDE1001 1.7 24.0 1.0
CAK A:RDE1001 2.7 23.2 1.0
CAT A:RDE1001 2.7 21.9 1.0
OAF A:RDE1001 3.0 21.2 1.0
ND2 A:ASN37 3.4 19.6 1.0
CD1 A:PHE124 3.4 15.0 1.0
O A:HOH1259 3.7 49.8 1.0
O A:HOH1209 3.8 46.7 1.0
CB A:PHE124 3.9 12.2 1.0
CG A:PHE124 3.9 13.5 1.0
CAX A:RDE1001 4.0 21.9 1.0
CAI A:RDE1001 4.0 19.9 1.0
CE1 A:PHE124 4.2 14.5 1.0
CD2 A:LEU93 4.2 19.6 1.0
CG A:ASN37 4.3 17.3 1.0
CB A:ASN37 4.4 17.4 1.0
CAU A:RDE1001 4.5 20.6 1.0
O A:HOH1208 4.5 55.0 1.0
O A:HOH1009 4.7 16.3 1.0
CA A:PHE124 4.9 12.9 1.0
CD2 A:PHE124 4.9 12.8 1.0

Reference:

R.M.Immormino, B.S.Blagg, D.T.Gewirth. Inhibitory Ligands Adopt Different Conformations When Bound to HSP90 or GRP94: Implications For Paralog-Specific Drug Design To Be Published.
Page generated: Sat Jul 20 04:52:42 2024

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