Potassium in PDB 6wsj: Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1, PDB code: 6wsj was solved by P.R.Watson, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	62.76 / 1.70
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.5, 84, 94.42, 90, 90, 90
R / Rfree (%)	15.4 / 17.6

The structure of Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1 also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Potassium atom in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1 (pdb code 6wsj). 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 Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1, PDB code: 6wsj:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1


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 Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1 within 5.0Å range: probe atom residue distance (Å) B Occ A:K802 b:7.4 occ:1.00 O A:ASP612 2.5 7.8 1.0 O A:LEU634 2.7 7.8 1.0 OD1 A:ASP610 2.7 8.8 1.0 O A:ASP610 2.8 8.2 1.0 O A:HIS614 2.8 6.9 1.0 OG A:SER633 2.8 7.7 1.0 CG A:ASP610 3.2 7.3 1.0 C A:ASP610 3.5 7.5 1.0 C A:ASP612 3.6 5.8 1.0 C A:HIS614 3.7 6.1 1.0 C A:LEU634 3.7 7.5 1.0 CB A:ASP610 3.8 6.0 1.0 N A:ASP612 3.9 6.9 1.0 OD2 A:ASP610 3.9 9.2 1.0 CB A:HIS635 3.9 7.0 1.0 CB A:SER633 4.0 8.1 1.0 N A:LEU634 4.0 7.7 1.0 CA A:ASP612 4.1 7.0 1.0 N A:TRP611 4.2 6.6 1.0 CA A:HIS615 4.2 4.5 1.0 C A:TRP611 4.2 6.1 1.0 CB A:ASP612 4.2 3.9 1.0 CA A:ASP610 4.3 5.9 1.0 N A:HIS615 4.3 4.8 1.0 ND1 A:HIS635 4.3 8.5 1.0 CA A:TRP611 4.3 5.3 1.0 CA A:SER633 4.3 8.3 1.0 N A:GLY616 4.4 8.9 1.0 CA A:HIS635 4.4 5.8 1.0 N A:HIS614 4.4 5.6 1.0 C A:SER633 4.5 7.7 1.0 N A:HIS635 4.5 7.3 1.0 CA A:LEU634 4.5 6.5 1.0 O A:HOH916 4.5 9.6 1.0 CG A:HIS635 4.6 7.8 1.0 C A:VAL613 4.7 8.4 1.0 C A:HIS615 4.7 6.9 1.0 OH A:TYR631 4.7 7.3 1.0 N A:VAL613 4.7 6.0 1.0 CA A:HIS614 4.7 4.2 1.0 CE1 A:HIS573 4.9 7.4 1.0 O A:TRP611 4.9 7.7 1.0 ND1 A:HIS573 4.9 7.0 1.0

Potassium binding site 2 out of 2 in the Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1


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 Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1 within 5.0Å range: probe atom residue distance (Å) B Occ A:K803 b:9.2 occ:1.00 O A:VAL629 2.6 9.9 1.0 O A:HOH971 2.7 8.8 1.0 O A:PHE623 2.7 8.1 1.0 O A:TYR662 2.8 7.2 1.0 O A:ASP626 2.9 13.3 1.0 O A:HOH1012 2.9 9.2 1.0 C A:TYR662 3.6 7.3 1.0 C A:PHE623 3.6 7.9 1.0 CB A:TYR662 3.7 9.8 1.0 CB A:PHE623 3.8 8.8 1.0 C A:VAL629 3.9 8.2 1.0 C A:ASP626 4.1 12.0 1.0 CA A:TYR662 4.3 8.2 1.0 N A:TYR631 4.3 6.5 1.0 CA A:PHE623 4.3 10.3 1.0 N A:ASN663 4.4 8.0 1.0 N A:ASP626 4.5 11.1 1.0 N A:GLU624 4.6 8.0 1.0 CA A:GLU624 4.6 8.0 1.0 CA A:LEU630 4.6 7.2 1.0 CA A:ASP626 4.7 9.5 1.0 CB A:ASP626 4.7 8.3 1.0 N A:LEU630 4.7 9.1 1.0 C A:GLU624 4.7 11.5 1.0 O A:GLU624 4.7 11.2 1.0 CA A:ASN663 4.8 7.6 1.0 CB A:ASN663 4.8 6.0 1.0 CB A:TYR631 4.8 8.0 1.0 O A:GLY659 4.8 10.9 1.0 C A:LEU630 4.9 9.2 1.0 CA A:VAL629 4.9 8.3 1.0 CG A:TYR662 5.0 8.8 1.0

P.R.Watson, D.W.Christianson. Crystal Structure of Danio Rerio Histone Deacetylase 6 Catalytic Domain 2 Complexed with Cyclopeptide DES4.3.1 To Be Published.