Chlorine in PDB 2wtw: Aurora-A Inhibitor Structure (2ND Crystal Form)

All present enzymatic activity of Aurora-A Inhibitor Structure (2ND Crystal Form):
2.7.11.1;

The structure of Aurora-A Inhibitor Structure (2ND Crystal Form), PDB code: 2wtw 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)	66.970 / 3.30
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	84.038, 84.038, 171.056, 90.00, 90.00, 120.00
R / Rfree (%)	23.39 / 28.83

The structure of Aurora-A Inhibitor Structure (2ND Crystal Form) also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Chlorine atom in the Aurora-A Inhibitor Structure (2ND Crystal Form) (pdb code 2wtw). 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 Aurora-A Inhibitor Structure (2ND Crystal Form), PDB code: 2wtw:

Chlorine binding site 1 out of 1 in the Aurora-A Inhibitor Structure (2ND Crystal Form)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Aurora-A Inhibitor Structure (2ND Crystal Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1390 b:71.0 occ:1.00 CL1 A:ZZL1390 0.0 71.0 1.0 C26 A:ZZL1390 1.8 71.0 1.0 C25 A:ZZL1390 2.8 71.0 1.0 C28 A:ZZL1390 2.8 71.0 1.0 CA A:GLY140 3.3 65.8 1.0 CG2 A:VAL147 3.5 65.2 1.0 C A:GLY140 3.7 65.8 1.0 N A:LYS141 3.7 94.1 1.0 C29 A:ZZL1390 4.1 71.0 1.0 C24 A:ZZL1390 4.1 71.0 1.0 N A:GLY140 4.3 65.8 1.0 O A:LYS141 4.3 94.1 1.0 CB A:VAL147 4.4 65.2 1.0 O A:GLY140 4.5 65.8 1.0 C30 A:ZZL1390 4.6 71.0 1.0 C A:LYS141 4.7 94.1 1.0 CA A:LYS141 4.7 94.1 1.0 O A:LEU139 4.9 62.0 1.0 C A:LEU139 4.9 62.0 1.0

C.A.Dodson, M.Kosmopoulou, M.W.Richards, B.Atrash, V.Bavetsias, J.Blagg, R.Bayliss. Crystal Structure of An Aurora-A Mutant That Mimics Aurora-B Bound to MLN8054: Insights Into Selectivity and Drug Design. Biochem.J. V. 427 19 2010.
ISSN: ISSN 0264-6021
PubMed: 20067443
DOI: 10.1042/BJ20091530