Potassium in PDB 3mz6: Crystal Structure of D101L FE2+ HDAC8 Complexed with M344

All present enzymatic activity of Crystal Structure of D101L FE2+ HDAC8 Complexed with M344:
3.5.1.98;

The structure of Crystal Structure of D101L FE2+ HDAC8 Complexed with M344, PDB code: 3mz6 was solved by D.P.Dowling, S.G.Gattis, C.A.Fierke, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	91.616, 87.561, 52.488, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 24.7

The structure of Crystal Structure of D101L FE2+ HDAC8 Complexed with M344 also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Potassium atom in the Crystal Structure of D101L FE2+ HDAC8 Complexed with M344 (pdb code 3mz6). 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 D101L FE2+ HDAC8 Complexed with M344, PDB code: 3mz6:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of D101L FE2+ HDAC8 Complexed with M344


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 D101L FE2+ HDAC8 Complexed with M344 within 5.0Å range: probe atom residue distance (Å) B Occ A:K401 b:20.5 occ:1.00 O A:ASP178 2.6 18.4 1.0 O A:LEU200 2.7 14.9 1.0 OD1 A:ASP176 2.7 17.5 1.0 O A:HIS180 2.8 14.4 1.0 O A:ASP176 2.9 17.0 1.0 OG A:SER199 2.9 18.7 1.0 N A:ASP178 3.4 16.3 1.0 CG A:ASP176 3.5 21.6 1.0 C A:ASP176 3.5 17.2 1.0 C A:ASP178 3.6 16.6 1.0 C A:LEU200 3.6 15.9 1.0 C A:HIS180 3.8 15.7 1.0 CB A:HIS201 3.8 15.3 1.0 CA A:ASP178 3.8 16.5 1.0 CB A:ASP178 3.9 14.3 1.0 C A:LEU177 3.9 18.2 1.0 CB A:ASP176 3.9 18.1 1.0 N A:LEU200 4.0 17.1 1.0 CB A:SER199 4.0 19.0 1.0 N A:LEU177 4.1 17.2 1.0 CA A:LEU177 4.1 16.1 1.0 ND1 A:HIS201 4.3 15.9 1.0 CA A:ASP176 4.3 18.8 1.0 CA A:SER199 4.3 19.1 1.0 CA A:HIS201 4.4 17.4 1.0 N A:GLY182 4.4 19.6 1.0 OD2 A:ASP176 4.4 20.5 1.0 N A:HIS180 4.4 15.2 1.0 CA A:HIS181 4.4 17.6 1.0 O A:HOH392 4.4 20.5 1.0 N A:HIS201 4.4 17.5 1.0 N A:HIS181 4.5 16.2 1.0 C A:SER199 4.5 18.2 1.0 CA A:LEU200 4.5 17.9 1.0 CG A:HIS201 4.5 19.6 1.0 C A:LEU179 4.6 17.1 1.0 O A:LEU177 4.7 17.8 1.0 C A:HIS181 4.7 18.6 1.0 N A:LEU179 4.7 16.0 1.0 CA A:HIS180 4.7 15.6 1.0 O A:LEU179 4.8 16.5 1.0 CE1 A:HIS142 4.9 18.3 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of D101L FE2+ HDAC8 Complexed with M344


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 D101L FE2+ HDAC8 Complexed with M344 within 5.0Å range: probe atom residue distance (Å) B Occ A:K402 b:26.0 occ:1.00 O A:VAL195 2.7 24.0 1.0 O A:PHE189 2.7 26.6 1.0 O A:HOH390 2.7 17.2 1.0 O A:THR192 2.9 25.1 1.0 O A:HOH391 2.9 21.4 1.0 O A:TYR225 3.0 24.9 1.0 CB A:TYR225 3.6 23.9 1.0 C A:TYR225 3.7 24.6 1.0 C A:PHE189 3.7 24.4 1.0 C A:VAL195 3.9 22.9 1.0 C A:THR192 4.0 28.4 1.0 OG A:SER226 4.0 25.9 1.0 CB A:PHE189 4.1 23.9 1.0 CA A:TYR225 4.2 24.4 1.0 CA A:SER190 4.4 28.7 1.0 N A:SER190 4.5 25.3 1.0 O A:SER190 4.5 28.0 1.0 N A:THR192 4.5 30.3 1.0 CA A:MET196 4.5 23.9 1.0 N A:SER226 4.5 24.1 1.0 CA A:PHE189 4.5 23.8 1.0 C A:SER190 4.5 28.3 1.0 O A:GLY222 4.5 26.1 1.0 CG2 A:THR192 4.6 29.4 1.0 N A:MET196 4.7 21.7 1.0 N A:THR197 4.7 24.5 1.0 CA A:THR192 4.7 28.8 1.0 CA A:GLY222 4.9 28.4 1.0 CA A:VAL195 4.9 24.4 1.0 CG A:TYR225 4.9 28.5 1.0 N A:VAL195 5.0 25.9 1.0 OG1 A:THR197 5.0 28.0 1.0 CA A:SER226 5.0 24.1 1.0

D.P.Dowling, S.G.Gattis, C.A.Fierke, D.W.Christianson. Structures of Metal-Substituted Human Histone Deacetylase 8 Provide Mechanistic Inferences on Biological Function. Biochemistry V. 49 5048 2010.
ISSN: ISSN 0006-2960
PubMed: 20545365
DOI: 10.1021/BI1005046