Chlorine in PDB 6ytg: CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3)

All present enzymatic activity of CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3):
2.7.12.1;

The structure of CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3), PDB code: 6ytg was solved by M.Schroeder, A.Chaikuad, K.Huber, 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)	67.46 / 1.95
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	92.928, 64.170, 80.809, 90.00, 123.41, 90.00
R / Rfree (%)	20.4 / 26.1

The binding sites of Chlorine atom in the CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) (pdb code 6ytg). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3), PDB code: 6ytg:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the CLK1 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 CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:21.3 occ:1.00 CL1 A:KHC501 0.0 21.3 1.0 C15 A:KHC501 1.7 15.8 1.0 C14 A:KHC501 2.7 16.0 1.0 C16 A:KHC501 2.7 16.2 1.0 C A:KHC501 3.0 16.2 1.0 CL A:KHC501 3.1 15.5 1.0 N A:KHC501 3.2 15.3 1.0 CD2 A:LEU295 3.7 15.6 1.0 CD1 A:LEU167 3.9 17.4 1.0 O A:HOH751 3.9 37.4 1.0 O A:LEU244 3.9 22.2 1.0 C13 A:KHC501 4.0 16.4 1.0 CB A:ALA189 4.0 14.6 1.0 C11 A:KHC501 4.0 16.2 1.0 N A:LEU244 4.2 17.5 1.0 CG1 A:VAL175 4.2 15.6 1.0 CB A:LEU244 4.3 18.0 1.0 C A:LEU244 4.4 20.9 1.0 C12 A:KHC501 4.5 16.0 1.0 CA A:LEU244 4.6 19.4 1.0 C1 A:KHC501 4.6 16.1 1.0 O A:GLY245 4.6 18.7 1.0 CB A:LEU167 4.6 18.2 1.0 CG A:LEU167 4.9 18.3 1.0 C10 A:KHC501 5.0 17.2 1.0

Chlorine binding site 2 out of 4 in the CLK1 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 CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:15.5 occ:1.00 CL A:KHC501 0.0 15.5 1.0 C14 A:KHC501 1.7 16.0 1.0 C13 A:KHC501 2.7 16.4 1.0 C15 A:KHC501 2.7 15.8 1.0 O A:GLU242 3.0 15.3 1.0 CL1 A:KHC501 3.1 21.3 1.0 CB A:PHE241 3.5 13.6 1.0 CB A:ALA189 3.6 14.6 1.0 CG A:LEU244 3.7 17.4 1.0 N A:LEU244 3.8 17.5 1.0 CB A:LEU244 3.9 18.0 1.0 CD1 A:LEU244 3.9 17.6 1.0 C12 A:KHC501 4.0 16.0 1.0 C16 A:KHC501 4.0 16.2 1.0 CG2 A:VAL225 4.0 14.6 1.0 CG A:PHE241 4.1 14.1 1.0 C A:GLU242 4.2 15.3 1.0 C A:LEU243 4.4 17.7 1.0 CA A:LEU244 4.5 19.4 1.0 C11 A:KHC501 4.5 16.2 1.0 CA A:LEU243 4.5 16.6 1.0 CD2 A:PHE241 4.5 14.3 1.0 CD2 A:LEU295 4.8 15.6 1.0 N A:LEU243 4.8 16.3 1.0 CA A:PHE241 4.8 13.9 1.0 CD1 A:PHE241 4.9 13.8 1.0 C A:PHE241 4.9 14.4 1.0 CA A:ALA189 5.0 14.2 1.0

Chlorine binding site 3 out of 4 in the CLK1 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 CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:36.4 occ:1.00 CL1 A:KHC502 0.0 36.4 1.0 C15 A:KHC502 1.8 33.1 1.0 C14 A:KHC502 2.7 31.1 1.0 C16 A:KHC502 2.8 28.4 1.0 C A:KHC502 3.1 25.7 1.0 CL A:KHC502 3.2 33.0 1.0 NE2 A:GLN208 3.3 33.8 1.0 N A:KHC502 3.3 29.2 1.0 CD A:GLN208 3.9 30.6 1.0 CB A:ARG204 4.0 26.3 1.0 C13 A:KHC502 4.0 31.2 1.0 C11 A:KHC502 4.1 29.7 1.0 C A:ARG204 4.3 22.0 1.0 O A:ARG204 4.4 21.0 1.0 OE1 A:GLN208 4.4 31.2 1.0 N A:SER205 4.5 21.1 1.0 C12 A:KHC502 4.6 29.7 1.0 O A:HOH648 4.6 21.6 1.0 CG A:GLN208 4.6 27.3 1.0 C1 A:KHC502 4.6 28.9 1.0 CA A:ARG204 4.8 23.2 1.0 CA A:SER205 4.9 20.5 1.0 CG A:ARG204 5.0 29.1 1.0

Chlorine binding site 4 out of 4 in the CLK1 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 CLK1 Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:33.0 occ:1.00 CL A:KHC502 0.0 33.0 1.0 C14 A:KHC502 1.7 31.1 1.0 C13 A:KHC502 2.7 31.2 1.0 C15 A:KHC502 2.7 33.1 1.0 CL1 A:KHC502 3.2 36.4 1.0 CB A:ARG204 3.6 26.3 1.0 CG A:ARG204 3.8 29.1 1.0 C12 A:KHC502 4.0 29.7 1.0 C16 A:KHC502 4.0 28.4 1.0 C11 A:KHC502 4.5 29.7 1.0 CD A:ARG204 4.8 29.4 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