Chlorine in PDB 2xne: Structure of Aurora-A Bound to An Imidazopyrazine Inhibitor

All present enzymatic activity of Structure of Aurora-A Bound to An Imidazopyrazine Inhibitor:
2.7.11.1;

The structure of Structure of Aurora-A Bound to An Imidazopyrazine Inhibitor, PDB code: 2xne was solved by M.Kosmopoulou, R.Bayliss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.99 / 2.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	82.923, 82.923, 167.092, 90.00, 90.00, 120.00
R / Rfree (%)	23.8 / 28.1

The binding sites of Chlorine atom in the Structure of Aurora-A Bound to An Imidazopyrazine Inhibitor (pdb code 2xne). 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 Aurora-A Bound to An Imidazopyrazine Inhibitor, PDB code: 2xne:

Chlorine binding site 1 out of 1 in the Structure of Aurora-A Bound to An Imidazopyrazine Inhibitor


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Aurora-A Bound to An Imidazopyrazine Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1389 b:71.4 occ:1.00 CL A:ASH1389 0.0 71.4 1.0 C02 A:ASH1389 1.7 75.2 1.0 N06 A:ASH1389 2.7 72.6 1.0 C03 A:ASH1389 2.7 72.2 1.0 C07 A:ASH1389 3.2 75.8 1.0 CD2 A:LEU194 3.7 57.6 1.0 CD1 A:LEU210 3.9 80.5 1.0 C05 A:ASH1389 3.9 67.1 1.0 N04 A:ASH1389 3.9 65.3 1.0 CG1 A:VAL147 4.0 83.0 1.0 CD1 A:LEU263 4.1 68.9 1.0 CB A:LEU210 4.3 79.8 1.0 CB A:ALA160 4.3 73.4 1.0 CG A:LEU210 4.6 77.1 1.0 C08 A:ASH1389 4.6 72.6 1.0 O A:GLU211 4.7 75.0 1.0 CG2 A:VAL147 4.9 79.4 1.0 CD2 A:LEU210 4.9 68.7 1.0

N.Bouloc, J.M.Large, M.Kosmopoulou, C.Sun, A.Faisal, M.Matteucci, J.Reynisson, N.Brown, B.Atrash, J.Blagg, E.Mcdonald, S.Linardopoulos, R.Bayliss, V.Bavetsias. Structure-Based Design of Imidazo[1,2-A]Pyrazine Derivatives As Selective Inhibitors of Aurora-A Kinase in Cells. Bioorg. Med. Chem. Lett. V. 20 5988 2010.
ISSN: ESSN 1464-3405
PubMed: 20833547
DOI: 10.1016/J.BMCL.2010.08.091