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Potassium in PDB 6z2v: CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3)Enzymatic activity of 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; Protein crystallography data
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:
Other elements in 6z2v:
The structure of CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3) also contains other interesting chemical elements:
Potassium Binding Sites:
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 6z2vGo back to Potassium Binding Sites List in 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
Reference:
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.
Page generated: Mon Dec 14 02:31:14 2020
ISSN: ISSN 0022-2623 PubMed: 32787076 DOI: 10.1021/ACS.JMEDCHEM.0C00898 |
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