Potassium in PDB 3qla: Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide

All present enzymatic activity of Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide:
3.6.4.12;

The structure of Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide, PDB code: 3qla was solved by B.Xiang, H.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.60 / 1.60
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	66.709, 66.709, 131.641, 90.00, 90.00, 120.00
R / Rfree (%)	15.7 / 17.9

The structure of Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide also contains other interesting chemical elements:

Zinc

(Zn)

6 atoms

The binding sites of Potassium atom in the Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide (pdb code 3qla). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide, PDB code: 3qla:

Potassium binding site 1 out of 1 in the Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Hexagonal Complex Structure of Atrx Add Bound to H3K9ME3 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:K290 b:22.7 occ:1.00 O A:ILE186 2.8 20.1 1.0 O D:HOH109 2.8 24.7 1.0 O D:MET205 2.8 17.6 1.0 O A:LYS183 2.8 28.4 1.0 O D:HOH453 3.0 42.4 1.0 O D:SER206 3.1 23.2 1.0 CZ A:TYR187 3.6 19.7 1.0 CE2 A:TYR187 3.6 17.6 1.0 C D:SER206 3.6 23.5 1.0 CD2 A:TYR187 3.7 13.4 1.0 CE1 A:TYR187 3.7 20.9 1.0 C A:LYS183 3.8 30.9 1.0 CG A:TYR187 3.8 14.7 1.0 CD1 A:TYR187 3.8 20.4 1.0 C A:ILE186 3.9 23.4 1.0 C D:MET205 4.0 14.4 1.0 CA D:SER206 4.1 14.5 1.0 CA A:ASP184 4.1 27.3 1.0 OH A:TYR187 4.1 21.7 1.0 C A:ASP184 4.4 27.2 1.0 N A:ASP184 4.4 27.5 1.0 N D:ASP207 4.4 15.8 1.0 OH A:TYR284 4.4 22.8 1.0 CA A:TYR187 4.5 18.0 1.0 N D:SER206 4.5 13.7 1.0 N A:ILE186 4.6 19.4 1.0 N A:TYR187 4.6 15.3 1.0 O D:HOH413 4.7 35.6 1.0 O A:ASP184 4.7 26.2 1.0 CA D:ASP207 4.7 17.2 1.0 CB A:TYR187 4.7 17.7 1.0 N A:SER185 4.8 22.7 1.0 CA A:LYS183 4.8 34.7 1.0 CA A:ILE186 4.9 20.5 1.0

S.Iwase, B.Xiang, S.Ghosh, T.Ren, P.W.Lewis, J.C.Cochrane, C.D.Allis, D.J.Picketts, D.J.Patel, H.Li, Y.Shi. Atrx Add Domain Links An Atypical Histone Methylation Recognition Mechanism to Human Mental-Retardation Syndrome Nat.Struct.Mol.Biol. V. 18 769 2011.
ISSN: ISSN 1545-9993
PubMed: 21666679
DOI: 10.1038/NSMB.2062