Chlorine in PDB 6khd: Crystal Structure of CLK1 in Complex with Cx-4945

All present enzymatic activity of Crystal Structure of CLK1 in Complex with Cx-4945:
2.7.12.1;

The structure of Crystal Structure of CLK1 in Complex with Cx-4945, PDB code: 6khd was solved by J.Y.Lee, J.S.Yun, H.Jin, J.H.Chang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.94 / 2.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.529, 115.675, 90.608, 90.00, 100.38, 90.00
R / Rfree (%)	20 / 27.4

The binding sites of Chlorine atom in the Crystal Structure of CLK1 in Complex with Cx-4945 (pdb code 6khd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of CLK1 in Complex with Cx-4945, PDB code: 6khd:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of CLK1 in Complex with Cx-4945


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of CLK1 in Complex with Cx-4945 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1000 b:0.7 occ:1.00 CL22 A:3NG1000 0.0 0.7 1.0 C18 A:3NG1000 1.7 97.7 1.0 C19 A:3NG1000 2.7 92.1 1.0 C17 A:3NG1000 2.7 87.3 1.0 CE1 A:PHE172 3.3 56.9 1.0 CZ A:PHE172 3.5 53.8 1.0 O A:GLU169 3.6 59.3 1.0 C A:GLU169 3.7 64.5 1.0 C A:GLY168 3.9 68.2 1.0 CG2 A:VAL175 3.9 49.4 1.0 N A:GLU169 3.9 71.2 1.0 O A:GLY168 3.9 66.0 1.0 C20 A:3NG1000 4.0 91.3 1.0 C16 A:3NG1000 4.0 84.1 1.0 CA A:GLU169 4.0 66.6 1.0 N A:GLY170 4.2 64.7 1.0 CB A:VAL175 4.4 49.4 1.0 N A:VAL175 4.5 48.2 1.0 CA A:GLY168 4.5 68.2 1.0 C21 A:3NG1000 4.5 87.2 1.0 O A:GLY173 4.5 56.2 1.0 CD1 A:PHE172 4.6 55.6 1.0 CA A:GLY170 4.7 52.2 1.0 CA A:LYS174 4.8 53.5 1.0 C A:LYS174 4.8 49.2 1.0 CE2 A:PHE172 4.9 55.1 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of CLK1 in Complex with Cx-4945


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of CLK1 in Complex with Cx-4945 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1000 b:0.7 occ:1.00 CL22 B:3NG1000 0.0 0.7 1.0 C18 B:3NG1000 1.7 97.7 1.0 C17 B:3NG1000 2.7 88.1 1.0 C19 B:3NG1000 2.7 0.2 1.0 O B:GLU169 3.5 76.3 1.0 N B:GLU169 3.5 73.7 1.0 C B:GLU169 3.7 69.7 1.0 CE1 B:PHE172 3.8 68.7 1.0 C B:GLY168 3.9 69.4 1.0 C16 B:3NG1000 4.0 87.8 1.0 CA B:GLU169 4.0 74.3 1.0 C20 B:3NG1000 4.0 96.6 1.0 CZ B:PHE172 4.1 69.4 1.0 CA B:GLY168 4.2 70.2 1.0 N B:GLY170 4.2 66.9 1.0 CG2 B:VAL175 4.4 61.1 1.0 C21 B:3NG1000 4.5 96.2 1.0 O B:GLY168 4.6 73.3 1.0 CA B:GLY170 4.8 67.7 1.0 CB B:VAL175 4.8 60.5 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of CLK1 in Complex with Cx-4945


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of CLK1 in Complex with Cx-4945 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1000 b:0.7 occ:1.00 CL22 C:3NG1000 0.0 0.7 1.0 C18 C:3NG1000 1.7 97.7 1.0 C19 C:3NG1000 2.7 90.4 1.0 C17 C:3NG1000 2.7 87.3 1.0 CE1 C:PHE172 3.2 73.5 1.0 O C:GLU169 3.4 72.1 1.0 CZ C:PHE172 3.4 68.8 1.0 C C:GLU169 3.7 63.6 1.0 C20 C:3NG1000 4.0 92.8 1.0 C16 C:3NG1000 4.0 84.0 1.0 N C:GLU169 4.1 69.2 1.0 C C:GLY168 4.1 68.8 1.0 N C:GLY170 4.2 61.2 1.0 CA C:GLU169 4.4 61.5 1.0 O C:GLY168 4.4 65.8 1.0 CG2 C:VAL175 4.4 52.6 1.0 C21 C:3NG1000 4.5 85.7 1.0 CA C:GLY170 4.5 58.1 1.0 CA C:GLY168 4.5 63.9 1.0 CD1 C:PHE172 4.5 70.5 1.0 CE2 C:PHE172 4.8 66.7 1.0 N C:VAL175 4.8 53.5 1.0 CA C:LYS174 4.9 57.7 1.0 CB C:VAL175 4.9 60.2 1.0

J.Y.Lee, J.S.Yun, W.K.Kim, H.S.Chun, H.Jin, S.Cho, J.H.Chang. Structural Basis For the Selective Inhibition of CDC2-Like Kinases By Cx-4945. Biomed Res Int V.2019 25068 2019.
ISSN: ESSN 2314-6141
PubMed: 31531359
DOI: 10.1155/2019/6125068