Bromine in PDB 6u80: Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction

The structure of Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction, PDB code: 6u80 was solved by B.Zhao, F.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.69 / 1.55
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	47.265, 46.812, 68.797, 89.21, 87.78, 75.17
R / Rfree (%)	17 / 20.3

The binding sites of Bromine atom in the Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction (pdb code 6u80). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction, PDB code: 6u80:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction within 5.0Å range: probe atom residue distance (Å) B Occ A:Br401 b:20.1 occ:1.00 BR6 A:Q1J401 0.0 20.1 1.0 C05 A:Q1J401 1.9 18.5 1.0 C07 A:Q1J401 2.8 20.9 1.0 C04 A:Q1J401 2.9 20.2 1.0 O A:TRP273 3.2 15.5 1.0 O A:SER267 3.6 16.1 1.0 N A:TRP273 3.7 14.9 1.0 N A:SER267 3.9 14.2 1.0 CB A:PHE266 3.9 13.8 1.0 CD2 A:PHE266 4.0 13.0 1.0 C A:TRP273 4.0 13.3 1.0 C A:LYS272 4.0 14.0 1.0 CA A:LYS272 4.0 17.4 1.0 CD2 A:LEU288 4.1 17.3 1.0 C08 A:Q1J401 4.1 19.6 1.0 CB A:LYS272 4.2 17.4 1.0 C03 A:Q1J401 4.2 16.8 1.0 CA A:PHE266 4.2 12.5 1.0 CD A:LYS272 4.2 22.7 1.0 CD1 A:LEU288 4.3 17.9 1.0 C A:SER267 4.3 16.2 1.0 C A:PHE266 4.4 13.0 1.0 CB A:LEU288 4.4 16.2 1.0 CG A:PHE266 4.5 15.0 1.0 CA A:TRP273 4.5 13.6 1.0 CG A:LEU288 4.5 14.8 1.0 CD1 A:ILE274 4.6 17.2 1.0 C09 A:Q1J401 4.7 18.5 1.0 CA A:SER267 4.7 15.5 1.0 O A:LYS272 4.8 16.3 1.0 O A:HOH611 4.8 17.8 1.0 CG A:LYS272 4.8 22.0 1.0 N A:ILE274 5.0 12.9 1.0

Bromine binding site 2 out of 2 in the Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Discovery and Optimization of Salicyclic Acid-Derived Sulfonamide Inhibitors of the WDR5:Myc Protein-Protein Interaction within 5.0Å range: probe atom residue distance (Å) B Occ B:Br401 b:33.1 occ:1.00 BR6 B:Q1J401 0.0 33.1 1.0 C05 B:Q1J401 1.9 36.6 1.0 C07 B:Q1J401 2.8 40.0 1.0 C04 B:Q1J401 2.9 38.0 1.0 O B:TRP273 3.3 17.0 1.0 O B:SER267 3.4 23.3 1.0 N B:TRP273 3.6 19.9 1.0 CD1 B:LEU288 3.7 28.7 1.0 CD2 B:PHE266 3.8 18.2 1.0 CB B:PHE266 3.9 17.6 1.0 CB B:LYS272 3.9 23.0 1.0 C B:LYS272 3.9 18.6 1.0 CA B:LYS272 3.9 22.3 1.0 N B:SER267 3.9 16.9 1.0 C B:SER267 4.1 19.1 1.0 C B:TRP273 4.1 16.9 1.0 C08 B:Q1J401 4.1 41.5 1.0 C03 B:Q1J401 4.2 39.3 1.0 CG B:LYS272 4.2 27.8 1.0 CA B:PHE266 4.2 16.9 1.0 C B:PHE266 4.3 18.2 1.0 CG B:PHE266 4.4 18.6 1.0 CA B:TRP273 4.5 18.0 1.0 CB B:LEU288 4.7 26.4 1.0 CA B:SER267 4.7 18.0 1.0 O B:LYS272 4.7 20.2 1.0 C09 B:Q1J401 4.7 42.5 1.0 O B:HOH559 4.7 33.7 1.0 CG1 B:VAL268 4.7 28.2 1.0 CG B:LEU288 4.7 29.3 1.0 CD B:LYS272 4.9 31.9 1.0 CE2 B:PHE266 4.9 22.6 1.0 N B:VAL268 5.0 20.0 1.0

J.D.Macdonald, S.Chacon Simon, C.Han, F.Wang, J.G.Shaw, J.E.Howes, J.Sai, J.Yuh, D.V.Camper, B.M.Alicie, J.Alvarado, S.Nikhar, W.G.Payne, E.R.Aho, J.Bauer, B.Zhao, J.Phan, L.R.Thomas, O.W.Rossanese, W.P.Tansey, A.G.Waterson, S.R.Stauffer, S.W.Fesik. Discovery and Optimization of Salicylic Acid-Derived Sulfonamide Inhibitors of the Wd Repeat-Containing Protein 5 (WDR5)-Myc Protein-Protein Interaction. J.Med.Chem. 2019.
ISSN: ISSN 0022-2623
PubMed: 31724864
DOI: 10.1021/ACS.JMEDCHEM.9B01411