Potassium in PDB 2vqj: Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor

The structure of Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor, PDB code: 2vqj was solved by M.J.Bottomley, P.Lo Surdo, P.Di Giovine, A.Cirillo, R.Scarpelli, F.Ferrigno, P.Jones, P.Neddermann, R.De Francesco, C.Steinkuhler, P.Gallinari, A.Carfi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	84.00 / 2.1
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	106.770, 137.562, 68.993, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 27.6

The structure of Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Zinc	(Zn)	2 atoms

The binding sites of Potassium atom in the Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor (pdb code 2vqj). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor, PDB code: 2vqj:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor within 5.0Å range: probe atom residue distance (Å) B Occ A:K1409 b:39.8 occ:1.00 O A:ASP196 2.5 26.0 1.0 OG A:SER217 2.7 28.7 1.0 O A:HIS198 2.9 28.0 1.0 O A:LEU218 2.9 28.0 1.0 OD1 A:ASP194 2.9 29.2 1.0 O A:ASP194 3.0 27.9 1.0 CG A:ASP194 3.4 29.6 1.0 C A:ASP196 3.6 27.1 1.0 C A:ASP194 3.6 28.2 1.0 C A:HIS198 3.7 27.6 1.0 C A:LEU218 3.7 29.1 1.0 CB A:HIS219 3.8 29.4 1.0 N A:ASP196 3.9 27.4 1.0 CB A:ASP194 4.0 28.5 1.0 CB A:SER217 4.0 29.7 1.0 N A:LEU218 4.1 29.6 1.0 CA A:HIS199 4.1 28.2 1.0 OD2 A:ASP194 4.1 30.4 1.0 CA A:ASP196 4.2 26.7 1.0 N A:HIS199 4.2 28.0 1.0 N A:GLY200 4.2 29.0 1.0 N A:TRP195 4.2 27.3 1.0 CB A:ASP196 4.3 26.8 1.0 C A:TRP195 4.3 27.4 1.0 CA A:TRP195 4.3 27.6 1.0 N A:HIS198 4.4 27.5 1.0 CA A:SER217 4.4 29.7 1.0 CA A:HIS219 4.4 29.3 1.0 CA A:ASP194 4.4 28.7 1.0 N A:HIS219 4.4 28.8 1.0 ND1 A:HIS219 4.5 29.0 1.0 C A:HIS199 4.5 28.4 1.0 C A:VAL197 4.5 27.0 1.0 C A:SER217 4.6 29.6 1.0 CG A:HIS219 4.6 28.3 1.0 CA A:LEU218 4.6 29.2 1.0 O A:HOH2152 4.6 24.1 1.0 CA A:HIS198 4.6 27.4 1.0 N A:VAL197 4.7 26.8 1.0 CE1 A:HIS158 4.7 27.6 1.0 O A:VAL197 4.9 27.7 1.0 ND1 A:HIS158 5.0 27.1 1.0 CA A:VAL197 5.0 26.8 1.0

Potassium binding site 2 out of 2 in the Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of HDAC4 Catalytic Domain Bound to A Trifluoromethylketone Inhbitor within 5.0Å range: probe atom residue distance (Å) B Occ A:K1410 b:54.5 occ:1.00 O A:VAL213 2.7 35.3 1.0 O A:PHE207 2.7 37.4 1.0 O A:HOH2140 2.8 34.3 1.0 O A:PHE244 3.0 39.4 1.0 O A:ASP210 3.0 44.5 1.0 O A:HOH2114 3.1 35.5 1.0 C A:PHE244 3.7 39.5 1.0 C A:PHE207 3.7 37.6 1.0 C A:VAL213 4.0 34.9 1.0 CB A:PHE244 4.0 40.9 1.0 CB A:PHE207 4.0 37.1 1.0 C A:ASP210 4.1 43.5 1.0 N A:ASN245 4.3 38.2 1.0 N A:TYR215 4.4 31.1 1.0 CG2 A:VAL213 4.4 36.0 1.0 O A:TYR208 4.4 41.5 1.0 CA A:TYR208 4.4 39.7 1.0 CA A:PHE244 4.4 40.5 1.0 N A:TYR208 4.5 38.4 1.0 CA A:PHE207 4.5 37.1 1.0 C A:TYR208 4.5 41.0 1.0 N A:ASP210 4.6 43.1 1.0 CA A:ASN245 4.6 36.9 1.0 CB A:ASN245 4.7 36.4 1.0 CB A:TYR215 4.7 30.5 1.0 ND2 A:ASN245 4.7 33.1 1.0 CA A:ASP210 4.8 43.3 1.0 CA A:LEU214 4.8 32.6 1.0 O A:GLY241 4.8 46.1 1.0 N A:LEU214 4.8 33.7 1.0 CB A:ASP210 4.9 42.9 1.0 CA A:VAL213 4.9 36.1 1.0

M.J.Bottomley, P.Lo Surdo, P.Di Giovine, A.Cirillo, R.Scarpelli, F.Ferrigno, P.Jones, P.Neddermann, R.De Francesco, C.Steinkuhler, P.Gallinari, A.Carfi. Structural and Functional Analysis of the Human HDAC4 Catalytic Domain Reveals A Regulatory Zinc-Binding Domain. J.Biol.Chem. V. 283 26694 2008.
ISSN: ISSN 0021-9258
PubMed: 18614528
DOI: 10.1074/JBC.M803514200