Chlorine in PDB 7s9f: Cryogenic Human HSP90A-Ntd Bound to BIIB021

All present enzymatic activity of Cryogenic Human HSP90A-Ntd Bound to BIIB021:
3.6.4.10;

The structure of Cryogenic Human HSP90A-Ntd Bound to BIIB021, PDB code: 7s9f was solved by T.R.Stachowski, M.Vanarotti, J.Seetharaman, M.Fischer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.10 / 2.30
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	70.28, 89.668, 97.948, 90, 90, 90
R / Rfree (%)	21.6 / 24.6

The structure of Cryogenic Human HSP90A-Ntd Bound to BIIB021 also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Chlorine atom in the Cryogenic Human HSP90A-Ntd Bound to BIIB021 (pdb code 7s9f). 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 Cryogenic Human HSP90A-Ntd Bound to BIIB021, PDB code: 7s9f:

Chlorine binding site 1 out of 1 in the Cryogenic Human HSP90A-Ntd Bound to BIIB021


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cryogenic Human HSP90A-Ntd Bound to BIIB021 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:28.3 occ:1.00 CL6 A:94M301 0.0 28.3 1.0 C6 A:94M301 1.8 27.6 1.0 N1 A:94M301 2.7 36.4 1.0 C5 A:94M301 2.8 27.9 1.0 HG22 A:ILE96 2.9 40.8 1.0 HG3 A:MET98 3.0 39.0 1.0 O A:GLY97 3.1 35.0 1.0 HB2 A:ALA55 3.2 39.5 1.0 H A:GLY97 3.2 34.4 1.0 HB1 A:ALA55 3.3 39.5 1.0 N7 A:94M301 3.3 26.1 1.0 O A:HOH427 3.3 33.0 1.0 C A:GLY97 3.5 29.8 1.0 HG23 A:ILE96 3.5 40.8 1.0 N A:GLY97 3.6 28.2 1.0 CG2 A:ILE96 3.6 33.5 1.0 CB A:ALA55 3.7 32.4 1.0 HA2 A:GLY97 3.7 39.0 1.0 CA A:GLY97 3.8 32.0 1.0 O A:HOH423 3.9 30.5 1.0 HE2 A:MET98 3.9 37.7 1.0 CG A:MET98 3.9 32.0 1.0 C2 A:94M301 3.9 27.9 1.0 HG21 A:ILE96 4.0 40.8 1.0 C4 A:94M301 4.0 30.5 1.0 O A:HOH433 4.0 36.0 1.0 HG2 A:MET98 4.1 39.0 1.0 HA A:ALA55 4.2 33.5 1.0 O A:HOH485 4.2 47.3 1.0 HB3 A:ALA55 4.4 39.5 1.0 N A:MET98 4.4 31.5 1.0 H A:ILE96 4.4 42.1 1.0 O A:HOH461 4.4 32.2 1.0 N3 A:94M301 4.5 24.2 1.0 OG1 A:THR184 4.5 27.9 1.0 C A:ILE96 4.6 30.5 1.0 CA A:ALA55 4.6 27.4 1.0 C8 A:94M301 4.6 26.9 1.0 HA A:MET98 4.7 34.4 1.0 SD A:MET98 4.7 27.0 1.0 CE A:MET98 4.7 30.9 1.0 HA3 A:GLY97 4.8 39.0 1.0 N A:ILE96 4.8 34.6 1.0 HG1 A:THR184 4.8 34.1 1.0 CB A:ILE96 4.9 31.4 1.0 CA A:MET98 4.9 28.2 1.0 N9 A:94M301 4.9 33.1 1.0 N2 A:94M301 5.0 34.3 1.0 CB A:MET98 5.0 31.6 1.0 H A:MET98 5.0 38.4 1.0 CA A:ILE96 5.0 36.2 1.0

T.R.Stachowski, M.Vanarotti, J.Seetharaman, K.Lopez, M.Fischer. Water Networks Repopulate Protein-Ligand Interfaces with Temperature. Angew.Chem.Int.Ed.Engl. V. 61 12919 2022.
ISSN: ESSN 1521-3773
PubMed: 35648650
DOI: 10.1002/ANIE.202112919