Potassium in PDB 7q1b: Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat

The structure of Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat, PDB code: 7q1b was solved by M.Marek, E.Ramos-Morales, C.Romier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.79 / 1.75
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	82.167, 93.584, 119.462, 90, 90, 90
R / Rfree (%)	19.2 / 21.8

The structure of Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Potassium atom in the Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat (pdb code 7q1b). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat, PDB code: 7q1b:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat within 5.0Å range: probe atom residue distance (Å) B Occ A:K602 b:28.1 occ:1.00 O A:MET259 2.6 24.8 1.0 O A:ASP237 2.6 25.7 1.0 O A:HIS239 2.6 23.2 1.0 OD1 A:ASP235 2.7 26.5 1.0 OG A:SER258 2.9 24.3 1.0 O A:ASP235 2.9 26.0 1.0 CG A:ASP235 3.3 28.8 1.0 C A:ASP235 3.5 26.4 1.0 C A:ASP237 3.6 28.3 1.0 C A:MET259 3.6 26.5 1.0 C A:HIS239 3.6 24.5 1.0 CB A:ASP235 3.8 27.5 1.0 N A:ASP237 3.9 24.6 1.0 N A:MET259 3.9 25.2 1.0 CB A:HIS260 4.0 25.5 1.0 N A:GLY241 4.1 25.2 1.0 CB A:SER258 4.1 26.9 1.0 OD2 A:ASP235 4.1 28.0 1.0 CA A:ASP237 4.1 26.0 1.0 N A:VAL236 4.2 27.3 1.0 N A:HIS239 4.2 25.1 1.0 CB A:ASP237 4.2 26.8 1.0 ND1 A:HIS260 4.2 26.6 1.0 C A:VAL236 4.3 26.7 1.0 CA A:ASP235 4.3 28.4 1.0 CA A:VAL236 4.3 25.8 1.0 CA A:SER258 4.3 28.1 1.0 CA A:HIS240 4.4 23.3 1.0 N A:HIS240 4.4 25.3 1.0 CA A:MET259 4.4 27.6 1.0 C A:SER258 4.4 30.3 1.0 C A:HIS240 4.5 24.6 1.0 N A:HIS260 4.5 25.2 1.0 CA A:HIS260 4.5 26.6 1.0 CA A:HIS239 4.6 24.9 1.0 CG A:HIS260 4.6 25.8 1.0 N A:ALA238 4.7 22.6 1.0 CE1 A:HIS197 4.7 26.3 1.0 C A:ALA238 4.7 26.2 1.0 OD1 A:ASP237 4.8 25.5 1.0 ND1 A:HIS197 4.9 25.2 1.0 CA A:GLY241 4.9 27.4 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of Trypanosoma Cruzi Histone Deacetylase DAC2 Complexed with Quisinostat within 5.0Å range: probe atom residue distance (Å) B Occ A:K603 b:35.2 occ:1.00 O A:VAL254 2.6 35.9 1.0 O A:PHE248 2.6 37.1 1.0 O A:HOH728 2.7 35.2 1.0 O A:ASP251 2.8 39.4 1.0 O A:HOH856 2.8 36.7 1.0 O A:PHE284 2.9 34.2 1.0 C A:PHE284 3.6 36.5 1.0 C A:PHE248 3.7 35.7 1.0 CB A:PHE284 3.7 40.0 1.0 C A:VAL254 3.8 37.6 1.0 CB A:PHE248 3.9 34.2 1.0 C A:ASP251 3.9 42.4 1.0 OG1 A:THR285 4.0 33.9 1.0 CA A:PHE284 4.3 39.1 1.0 N A:ASP251 4.3 40.2 1.0 N A:THR285 4.3 35.0 1.0 CA A:LEU255 4.4 34.9 1.0 CA A:PHE248 4.4 35.9 1.0 N A:THR256 4.4 32.6 1.0 CB A:ASP251 4.4 41.8 1.0 CA A:ASP251 4.4 42.3 1.0 N A:LEU255 4.6 35.0 1.0 N A:LEU249 4.6 35.5 1.0 O A:LEU249 4.6 38.4 1.0 C A:LEU249 4.7 38.2 1.0 CA A:LEU249 4.7 39.5 1.0 O A:GLY281 4.7 38.7 1.0 OG1 A:THR256 4.8 31.4 1.0 CA A:THR285 4.8 34.0 1.0 CG2 A:THR256 4.9 31.2 1.0 CA A:VAL254 4.9 39.7 1.0 C A:LEU255 4.9 36.1 1.0 CA A:GLY281 5.0 40.2 1.0 CG A:PHE284 5.0 42.9 1.0 N A:ASN252 5.0 43.1 1.0 CB A:THR285 5.0 35.4 1.0

M.Marek, E.Ramos-Morales, C.Romier. Species-Selective Targeting of Pathogens Revealed By the Atypical Structure and Active Site of Trypanosoma Cruzi Histone Deacetylase DAC2 To Be Published.