Chlorine in PDB 2e9u: Structure of H-CHK1 Complexed with A780125

All present enzymatic activity of Structure of H-CHK1 Complexed with A780125:
2.7.11.1;

The structure of Structure of H-CHK1 Complexed with A780125, PDB code: 2e9u was solved by C.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.72 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	45.075, 65.820, 57.945, 90.00, 94.37, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Structure of H-CHK1 Complexed with A780125 (pdb code 2e9u). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of H-CHK1 Complexed with A780125, PDB code: 2e9u:

Chlorine binding site 1 out of 1 in the Structure of H-CHK1 Complexed with A780125


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of H-CHK1 Complexed with A780125 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1001 b:38.7 occ:1.00 CL7 A:A251001 0.0 38.7 1.0 C5 A:A251001 1.7 38.7 1.0 C4 A:A251001 2.7 38.7 1.0 C6 A:A251001 2.7 38.8 1.0 O A:CYS87 3.4 37.5 1.0 O A:HOH1248 3.5 60.6 1.0 CA A:GLY90 3.6 32.9 1.0 O A:SER88 3.7 35.9 1.0 N A:GLY90 3.7 33.5 1.0 C A:SER88 4.0 35.9 1.0 O A:HOH1251 4.0 59.0 1.0 O A:HOH1147 4.0 60.6 1.0 C1 A:A251001 4.0 38.7 1.0 CA A:SER88 4.0 36.4 1.0 C3 A:A251001 4.0 38.6 1.0 CD2 A:LEU15 4.2 59.9 1.0 CE1 A:TYR86 4.3 39.9 1.0 C A:CYS87 4.4 37.6 1.0 OH A:TYR86 4.4 39.8 1.0 C2 A:A251001 4.6 38.7 1.0 O A:HOH1245 4.6 53.5 1.0 N A:SER88 4.7 37.0 1.0 C A:GLY89 4.7 33.9 1.0 N A:GLY89 4.8 35.3 1.0 CZ A:TYR86 4.8 39.8 1.0 O13 A:A251001 4.9 38.6 1.0 C A:GLY90 5.0 32.4 1.0

Y.Tong, A.Claiborne, K.D.Stewart, C.Park, P.Kovar, Z.Chen, R.B.Credo, S.L.Gwaltney, H.Zhang, S.H.Rosenberg, H.L.Sham, T.J.Sowin, N.H.Lin. Structure-Based Design, Synthesis and Biological Evaluation of Potent Selective Macrocyclic CHK1 Inhibitors To Be Published.