Chlorine in PDB 6yu1: CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3)

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

The structure of CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3), PDB code: 6yu1 was solved by M.Schroeder, A.Chaikuad, S.Knapp, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	75.13 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	96.269, 131.030, 83.620, 90.00, 107.71, 90.00
R / Rfree (%)	17.6 / 20.3

The binding sites of Chlorine atom in the CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) (pdb code 6yu1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3), PDB code: 6yu1:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ a:Cl510 b:75.4 occ:1.00 CL1 a:KHC510 0.0 75.4 1.0 C15 a:KHC510 1.7 67.7 1.0 C16 a:KHC510 2.7 67.3 1.0 C14 a:KHC510 2.7 66.7 1.0 C a:KHC510 3.0 57.3 1.0 CL a:KHC510 3.1 78.0 1.0 N a:KHC510 3.2 62.4 1.0 CD1 a:PHE236 3.4 28.4 1.0 CG a:PHE236 3.8 28.5 1.0 CE1 a:PHE236 3.9 28.1 1.0 C13 a:KHC510 4.0 62.8 1.0 C11 a:KHC510 4.0 65.9 1.0 CB a:ALA184 4.0 30.1 1.0 CB a:PHE236 4.2 28.9 1.0 C12 a:KHC510 4.5 62.1 1.0 C1 a:KHC510 4.5 66.0 1.0 CD2 a:PHE236 4.6 29.2 1.0 O a:HOH755 4.7 49.7 1.0 CZ a:PHE236 4.7 27.7 1.0 CG1 a:VAL170 4.9 31.4 1.0 C10 a:KHC510 5.0 64.9 1.0

Chlorine binding site 2 out of 4 in the CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ a:Cl510 b:78.0 occ:1.00 CL a:KHC510 0.0 78.0 1.0 C14 a:KHC510 1.7 66.7 1.0 C13 a:KHC510 2.7 62.8 1.0 C15 a:KHC510 2.7 67.7 1.0 CL1 a:KHC510 3.1 75.4 1.0 CG2 a:VAL170 3.6 30.8 1.0 CD a:LYS186 3.8 32.7 1.0 C12 a:KHC510 4.0 62.1 1.0 C16 a:KHC510 4.0 67.3 1.0 CE a:LYS186 4.1 36.4 1.0 CG1 a:VAL170 4.2 31.4 1.0 CG a:LYS186 4.3 31.2 1.0 CB a:LYS186 4.5 28.6 1.0 CB a:VAL170 4.5 31.3 1.0 C11 a:KHC510 4.5 65.9 1.0 NZ a:LYS186 4.8 38.5 1.0

Chlorine binding site 3 out of 4 in the CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ c:Cl519 b:75.7 occ:1.00 CL1 c:KHC519 0.0 75.7 1.0 C15 c:KHC519 1.7 65.7 1.0 C14 c:KHC519 2.7 67.8 1.0 C16 c:KHC519 2.7 59.8 1.0 C c:KHC519 3.1 48.6 1.0 CL c:KHC519 3.1 78.8 1.0 N c:KHC519 3.3 53.0 1.0 CD2 c:PHE236 3.4 23.4 1.0 CE2 c:PHE236 3.8 24.1 1.0 CB c:ALA184 4.0 21.9 1.0 CG c:PHE236 4.0 23.2 1.0 C13 c:KHC519 4.0 58.7 1.0 C11 c:KHC519 4.0 55.5 1.0 CB c:PHE236 4.4 22.8 1.0 C12 c:KHC519 4.5 55.5 1.0 CG c:LYS186 4.6 29.2 1.0 C1 c:KHC519 4.6 51.1 1.0 CZ c:PHE236 4.7 24.8 1.0 CG1 c:VAL170 4.7 25.6 1.0 CD1 c:PHE236 4.9 24.2 1.0 O c:ALA184 4.9 21.2 1.0 C10 c:KHC519 5.0 52.7 1.0

Chlorine binding site 4 out of 4 in the CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of CLK3 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ c:Cl519 b:78.8 occ:1.00 CL c:KHC519 0.0 78.8 1.0 C14 c:KHC519 1.7 67.8 1.0 C13 c:KHC519 2.7 58.7 1.0 C15 c:KHC519 2.7 65.7 1.0 CL1 c:KHC519 3.1 75.7 1.0 CD c:LYS186 3.5 31.4 1.0 CG2 c:VAL170 3.6 26.1 1.0 CG c:LYS186 3.7 29.2 1.0 C12 c:KHC519 4.0 55.5 1.0 C16 c:KHC519 4.0 59.8 1.0 CG1 c:VAL170 4.4 25.6 1.0 CE c:LYS186 4.5 33.4 1.0 C11 c:KHC519 4.5 55.5 1.0 NZ c:LYS186 4.5 32.3 1.0 CB c:VAL170 4.6 25.5 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