Potassium in PDB 4bkx: The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex

All present enzymatic activity of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex:
3.5.1.98;

The structure of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex, PDB code: 4bkx was solved by C.J.Millard, P.J.Watson, I.Celardo, Y.Gordiyenko, S.M.Cowley, C.V.Robinson, L.Fairall, J.W.R.Schwabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.75 / 3.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.199, 108.199, 133.164, 90.00, 90.00, 120.00
R / Rfree (%)	21.084 / 26.149

The structure of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Potassium atom in the The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex (pdb code 4bkx). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex, PDB code: 4bkx:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:K602 b:50.4 occ:1.00 O B:ASP176 2.6 43.3 1.0 OD1 B:ASP174 2.7 50.3 1.0 OG B:SER197 2.9 45.8 1.0 O B:ASP174 3.1 46.4 1.0 O B:HIS178 3.1 44.2 1.0 O B:PHE198 3.1 47.7 1.0 CG B:ASP174 3.6 49.1 1.0 C B:ASP176 3.7 43.0 1.0 N B:PHE198 3.7 44.2 1.0 C B:PHE198 3.7 46.3 1.0 C B:ASP174 3.8 46.5 1.0 C B:HIS178 3.9 44.7 1.0 CB B:HIS199 3.9 50.7 1.0 N B:ASP176 4.0 44.7 1.0 CB B:ASP174 4.0 47.6 1.0 ND1 B:HIS199 4.1 52.3 1.0 CB B:SER197 4.1 44.6 1.0 N B:GLY180 4.1 48.8 1.0 CA B:HIS179 4.1 46.5 1.0 C B:ILE175 4.2 46.1 1.0 CA B:ASP176 4.2 43.3 1.0 CB B:ASP176 4.4 42.3 1.0 CA B:SER197 4.4 44.2 1.0 N B:HIS179 4.4 45.7 1.0 CA B:PHE198 4.4 44.5 1.0 N B:HIS199 4.4 47.6 1.0 C B:SER197 4.4 44.3 1.0 CA B:HIS199 4.5 49.1 1.0 CG B:HIS199 4.5 52.0 1.0 N B:ILE175 4.5 46.2 1.0 OD2 B:ASP174 4.5 49.2 1.0 C B:HIS179 4.5 47.7 1.0 CA B:ASP174 4.6 46.2 1.0 O B:ILE175 4.6 46.4 1.0 C B:ILE177 4.7 42.8 1.0 CA B:ILE175 4.7 46.3 1.0 N B:HIS178 4.7 43.4 1.0 N B:ILE177 4.8 42.3 1.0 O B:ILE177 4.9 43.3 1.0 CE1 B:HIS140 4.9 49.9 1.0 CA B:HIS178 4.9 44.0 1.0

Potassium binding site 2 out of 2 in the The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of The Structure of HDAC1 in Complex with the Dimeric ELM2-Sant Domain of MTA1 From the Nurd Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:K603 b:0.3 occ:1.00 O B:PHE187 2.8 58.9 1.0 O B:VAL193 3.2 58.3 1.0 O B:TYR222 3.2 58.4 1.0 O B:THR190 3.6 60.6 1.0 C B:PHE187 3.7 59.4 1.0 C B:TYR222 3.9 59.2 1.0 CB B:TYR222 4.1 62.0 1.0 CA B:TYR188 4.3 58.3 1.0 O B:GLY219 4.3 70.0 1.0 CB B:ALA223 4.3 55.0 1.0 CB B:PHE187 4.4 61.9 1.0 N B:TYR188 4.4 59.3 1.0 O B:TYR188 4.4 58.9 1.0 C B:VAL193 4.4 56.8 1.0 C B:TYR188 4.4 58.3 1.0 N B:ALA223 4.5 56.7 1.0 OG1 B:THR195 4.6 51.4 1.0 CA B:TYR222 4.6 61.6 1.0 CG2 B:THR195 4.6 50.8 1.0 CA B:ALA223 4.6 55.0 1.0 N B:THR195 4.6 50.0 1.0 CA B:PHE187 4.7 60.2 1.0 CA B:GLY219 4.7 67.3 1.0 C B:THR190 4.8 60.2 1.0 CA B:MET194 4.8 51.8 1.0 N B:THR190 4.9 58.2 1.0 O B:GLU184 4.9 59.5 1.0 C B:GLY219 5.0 68.5 1.0

C.J.Millard, P.J.Watson, I.Celardo, Y.Gordiyenko, S.M.Cowley, C.V.Robinson, L.Fairall, J.W.R.Schwabe. Class I Hdacs Share A Common Mechanism of Regulation By Inositol Phosphates. Mol.Cell V. 51 57 2013.
ISSN: ISSN 1097-2765
PubMed: 23791785
DOI: 10.1016/J.MOLCEL.2013.05.020