Potassium in PDB 6z2v: CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3)

All present enzymatic activity of CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3):
2.7.12.1;

The structure of CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3), PDB code: 6z2v was solved by M.Schroeder, A.Chaikuad, F.Bracher, S.Knapp, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.37 / 2.60
Space group	I 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.376, 45.393, 106.334, 90.00, 111.16, 90.00
R / Rfree (%)	20.2 / 26.5

The structure of CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3) also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Potassium atom in the CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3) (pdb code 6z2v). 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 CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3), PDB code: 6z2v:

Potassium binding site 1 out of 1 in the CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:K502 b:41.1 occ:1.00 NE2 A:HIS339 2.4 31.6 1.0 NE2 A:HIS377 2.8 40.0 1.0 CE1 A:HIS377 2.8 39.6 1.0 CE1 A:HIS339 3.3 33.2 1.0 CD2 A:HIS339 3.5 29.9 1.0 CD2 A:HIS377 4.1 39.0 1.0 ND1 A:HIS377 4.2 39.4 1.0 ND1 A:HIS339 4.5 31.8 1.0 CG A:HIS339 4.6 29.6 1.0 CG A:HIS377 4.8 38.4 1.0

M.Schroder, A.N.Bullock, O.Fedorov, F.Bracher, A.Chaikuad, S.Knapp. Dfg-1 Residue Controls Inhibitor Binding Mode and Affinity, Providing A Basis For Rational Design of Kinase Inhibitor Selectivity. J.Med.Chem. V. 63 10224 2020.
ISSN: ISSN 0022-2623
PubMed: 32787076
DOI: 10.1021/ACS.JMEDCHEM.0C00898