Zinc in PDB 7ao8: Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex

All present enzymatic activity of Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex:
3.5.1.98;

The structure of Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex also contains other interesting chemical elements:

Potassium

(K)

4 atoms

The binding sites of Zinc atom in the Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex (pdb code 7ao8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex, PDB code: 7ao8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn501 b:24.9 occ:1.00 OD2 E:ASP264 1.9 14.5 1.0 OD1 E:ASP176 2.0 26.2 1.0 ND1 E:HIS178 2.1 27.8 1.0 CG E:ASP176 2.8 26.6 1.0 CG E:ASP264 2.8 14.8 1.0 OD2 E:ASP176 3.0 27.2 1.0 CG E:HIS178 3.0 27.9 1.0 OD1 E:ASP264 3.1 15.0 1.0 CE1 E:HIS178 3.1 27.9 1.0 CB E:HIS178 3.3 28.0 1.0 N E:HIS178 3.6 27.4 1.0 CG2 E:ILE177 3.9 25.1 1.0 CA E:HIS178 4.1 27.9 1.0 CA E:GLY301 4.2 21.8 1.0 CD2 E:HIS178 4.2 27.7 1.0 CB E:ASP176 4.2 26.9 1.0 NE2 E:HIS178 4.2 27.5 1.0 CB E:ASP264 4.2 14.9 1.0 N E:ILE177 4.4 26.2 1.0 NE2 E:HIS140 4.4 38.2 1.0 NE2 E:HIS141 4.6 44.2 1.0 C E:ILE177 4.6 26.4 1.0 N E:GLY301 4.6 21.9 1.0 CE2 E:TYR303 4.8 23.0 1.0 CA E:ILE177 4.8 25.7 1.0 C E:ASP176 4.8 26.8 1.0 CA E:ASP176 4.9 27.4 1.0 OH E:TYR303 4.9 25.2 1.0 O E:HIS178 5.0 28.5 1.0 CB E:ILE177 5.0 25.0 1.0

Zinc binding site 2 out of 2 in the Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the MTA1/HDAC1/MBD2 Nurd Deacetylase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:24.9 occ:1.00 OD2 B:ASP264 1.9 14.5 1.0 OD1 B:ASP176 2.0 26.2 1.0 ND1 B:HIS178 2.1 27.8 1.0 CG B:ASP176 2.8 26.6 1.0 CG B:ASP264 2.8 14.8 1.0 OD2 B:ASP176 3.0 27.2 1.0 CG B:HIS178 3.0 27.9 1.0 OD1 B:ASP264 3.1 15.0 1.0 CE1 B:HIS178 3.1 27.9 1.0 CB B:HIS178 3.3 28.0 1.0 N B:HIS178 3.6 27.4 1.0 CG2 B:ILE177 3.9 25.1 1.0 CA B:HIS178 4.1 27.9 1.0 CA B:GLY301 4.2 21.8 1.0 CD2 B:HIS178 4.2 27.7 1.0 CB B:ASP176 4.2 26.9 1.0 NE2 B:HIS178 4.2 27.5 1.0 CB B:ASP264 4.2 14.9 1.0 N B:ILE177 4.4 26.2 1.0 NE2 B:HIS140 4.4 38.2 1.0 NE2 B:HIS141 4.6 44.2 1.0 C B:ILE177 4.6 26.4 1.0 N B:GLY301 4.6 21.9 1.0 CE2 B:TYR303 4.8 23.0 1.0 CA B:ILE177 4.8 25.7 1.0 C B:ASP176 4.8 26.8 1.0 CA B:ASP176 4.9 27.4 1.0 OH B:TYR303 4.9 25.2 1.0 O B:HIS178 5.0 28.5 1.0 CB B:ILE177 5.0 25.0 1.0

C.J.Millard, L.Fairall, T.J.Ragan, C.G.Savva, J.W.R.Schwabe. The Topology of Chromatin-Binding Domains in the Nurd Deacetylase Complex To Be Published.