Chlorine 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:

Potassium

(K)

1 atom

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the CLK3 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3), PDB code: 6z2v:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the CLK3 A319V Mutant 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 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:52.2 occ:1.00 CL1 A:KHC501 0.0 52.2 1.0 C15 A:KHC501 1.7 55.5 1.0 C14 A:KHC501 2.7 52.3 1.0 C16 A:KHC501 2.7 57.6 1.0 C A:KHC501 3.0 50.4 1.0 CL A:KHC501 3.1 45.4 1.0 N A:KHC501 3.2 54.4 1.0 O A:LEU239 3.7 35.4 1.0 N A:LEU239 3.8 35.8 1.0 CD1 A:LEU290 3.8 25.6 1.0 C13 A:KHC501 4.0 52.6 1.0 C11 A:KHC501 4.0 58.0 1.0 CD1 A:LEU238 4.2 37.8 1.0 CB A:LEU239 4.3 33.8 1.0 C A:LEU239 4.3 35.5 1.0 CB A:ALA184 4.3 33.8 1.0 CA A:LEU239 4.4 35.2 1.0 C12 A:KHC501 4.5 53.8 1.0 C1 A:KHC501 4.6 59.8 1.0 O A:GLY240 4.7 32.4 1.0 C A:LEU238 4.8 38.9 1.0 CA A:LEU238 4.8 39.2 1.0 C10 A:KHC501 5.0 62.8 1.0

Chlorine binding site 2 out of 2 in the CLK3 A319V Mutant 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 A319V Mutant Bound with Beta-Carboline Kh-CARB13 (Cpd 3) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:45.4 occ:1.00 CL A:KHC501 0.0 45.4 1.0 C14 A:KHC501 1.7 52.3 1.0 O A:GLU237 2.5 39.5 1.0 C13 A:KHC501 2.7 52.6 1.0 C15 A:KHC501 2.7 55.5 1.0 CL1 A:KHC501 3.1 52.2 1.0 N A:LEU239 3.5 35.8 1.0 C A:GLU237 3.6 42.2 1.0 CG A:LEU239 3.6 34.0 1.0 CD1 A:LEU239 3.8 32.3 1.0 CB A:LEU239 3.9 33.8 1.0 CA A:LEU238 3.9 39.2 1.0 C A:LEU238 3.9 38.9 1.0 C12 A:KHC501 4.0 53.8 1.0 C16 A:KHC501 4.0 57.6 1.0 CB A:ALA184 4.0 33.8 1.0 CB A:PHE236 4.1 38.2 1.0 N A:LEU238 4.1 40.7 1.0 CA A:LEU239 4.3 35.2 1.0 CG2 A:VAL220 4.5 31.8 1.0 C11 A:KHC501 4.5 58.0 1.0 C A:PHE236 4.6 39.2 1.0 O A:PHE236 4.6 38.6 1.0 N A:GLU237 4.7 41.9 1.0 CA A:GLU237 4.8 45.8 1.0 CD1 A:LEU290 4.8 25.6 1.0 CG A:GLU237 4.8 50.8 1.0 O A:LEU238 4.8 42.1 1.0 CG A:PHE236 4.9 38.7 1.0 CD2 A:LEU239 5.0 35.2 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