Chlorine in PDB 2vag: Crystal Structure of Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor

All present enzymatic activity of Crystal Structure of Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor:
2.7.12.1;

The structure of Crystal Structure of Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor, PDB code: 2vag was solved by A.C.W.Pike, A.N.Bullock, O.Fedorov, E.S.Pilka, E.Ugochukwu, F.Von Delft, A.Edwards, C.H.Arrowsmith, J.Weigelt, M.Sundstrom, K.Huber, F.Bracher, S.Knapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.00 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.950, 64.108, 78.894, 90.00, 118.17, 90.00
R / Rfree (%)	18 / 22.5

The binding sites of Chlorine atom in the Crystal Structure of Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor (pdb code 2vag). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor, PDB code: 2vag:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor


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 Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1482 b:30.6 occ:1.00 CL1 A:V251482 0.0 30.6 1.0 CAQ A:V251482 1.7 10.8 1.0 CAP A:V251482 2.6 13.1 1.0 CAU A:V251482 2.7 9.9 1.0 CL2 A:V251482 3.1 12.4 1.0 CAB A:V251482 3.1 14.6 1.0 NAV A:V251482 3.3 10.6 1.0 CD1 A:LEU167 3.6 13.2 1.0 CB A:ALA189 3.6 10.4 1.0 O A:LEU244 3.8 24.4 1.0 CD2 A:LEU295 3.9 14.6 1.0 CAJ A:V251482 3.9 9.9 1.0 CAT A:V251482 4.0 2.1 1.0 N A:LEU244 4.1 15.6 1.0 CG1 A:VAL175 4.2 11.7 1.0 C A:LEU244 4.4 20.2 1.0 CB A:LEU244 4.4 17.8 1.0 CAK A:V251482 4.5 5.8 1.0 CA A:LEU244 4.5 20.7 1.0 CD1 A:LEU243 4.6 21.0 1.0 CAS A:V251482 4.6 8.3 1.0 CB A:LEU167 4.7 12.3 1.0 CG A:LEU167 4.8 6.8 1.0 O A:GLY245 4.8 19.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor


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 Di-Phosphorylated Human CLK1 in Complex with A Novel Substituted Indole Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1482 b:12.4 occ:1.00 CL2 A:V251482 0.0 12.4 1.0 CAP A:V251482 1.7 13.1 1.0 CAJ A:V251482 2.7 9.9 1.0 CAQ A:V251482 2.7 10.8 1.0 O A:GLU242 2.9 19.2 1.0 CL1 A:V251482 3.1 30.6 1.0 CB A:PHE241 3.5 13.2 1.0 CB A:ALA189 3.6 10.4 1.0 N A:LEU244 3.7 15.6 1.0 CG A:LEU244 3.8 20.3 1.0 CD1 A:LEU244 3.9 17.5 1.0 CB A:LEU244 4.0 17.8 1.0 CAK A:V251482 4.0 5.8 1.0 CG2 A:VAL225 4.0 30.6 1.0 CAU A:V251482 4.0 9.9 1.0 C A:GLU242 4.1 17.6 1.0 CG A:PHE241 4.2 12.4 1.0 C A:LEU243 4.4 15.3 1.0 CA A:LEU243 4.4 12.8 1.0 CD2 A:PHE241 4.4 13.4 1.0 CA A:LEU244 4.5 20.7 1.0 CAT A:V251482 4.5 2.1 1.0 CD2 A:LEU295 4.7 14.6 1.0 C A:PHE241 4.7 10.4 1.0 N A:LEU243 4.7 11.4 1.0 CA A:PHE241 4.8 8.9 1.0 O A:PHE241 4.9 9.8 1.0 CA A:ALA189 5.0 8.0 1.0

O.Fedorov, K.Huber, A.Eisenreich, P.Filippakopoulos, O.King, A.N.Bullock, D.Szklarczyk, L.J.Jensen, D.Fabbro, J.Trappe, U.Rauch, F.Bracher, S.Knapp. Specific Clk Inhibitors From A Novel Chemotype For Regulation of Alternative Splicing. Chem.Biol V. 18 67 2011.
ISSN: ISSN 1074-5521
PubMed: 21276940
DOI: 10.1016/J.CHEMBIOL.2010.11.009