Potassium in PDB 5kik: Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State

The structure of Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State, PDB code: 5kik was solved by C.J.Knoot, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.88 / 2.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	153.529, 153.529, 93.043, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 21.3

The structure of Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Potassium atom in the Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State (pdb code 5kik). 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 Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State, PDB code: 5kik:

Potassium binding site 1 out of 1 in the Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State within 5.0Å range: probe atom residue distance (Å) B Occ A:K603 b:56.9 occ:1.00 O A:HOH868 2.7 69.5 1.0 O A:SER150 2.7 48.2 1.0 O A:TYR153 2.7 44.3 1.0 O A:TYR148 2.9 44.0 1.0 O A:HOH876 3.2 76.4 1.0 O A:ALA149 3.7 56.2 1.0 C A:ALA149 3.7 46.6 1.0 C A:SER150 3.8 47.3 1.0 O A:HOH842 3.8 59.4 1.0 C A:TYR153 3.9 41.9 1.0 C A:TYR148 4.0 45.5 1.0 CD2 A:TYR153 4.1 38.4 1.0 CA A:ALA149 4.1 45.0 1.0 N A:SER150 4.1 48.2 1.0 CB A:TYR153 4.1 40.0 1.0 CA A:TYR153 4.4 45.8 1.0 N A:ALA149 4.5 45.3 1.0 CA A:SER150 4.5 44.7 1.0 CG A:TYR153 4.6 38.5 1.0 N A:TYR153 4.6 41.8 1.0 N A:GLU151 4.7 45.2 1.0 CA A:GLU151 4.8 47.9 1.0 N A:ASP154 5.0 47.7 1.0

A.J.Jasniewski, C.J.Knoot, J.D.Lipscomb, L.Que. A Carboxylate Shift Regulates Dioxygen Activation By the Diiron Nonheme Beta-Hydroxylase Cmla Upon Binding of A Substrate-Loaded Nonribosomal Peptide Synthetase. Biochemistry V. 55 5818 2016.
ISSN: ISSN 1520-4995
PubMed: 27668828
DOI: 10.1021/ACS.BIOCHEM.6B00834