Bromine in PDB 2x6e: Aurora-A Bound to An Inhibitor

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

The structure of Aurora-A Bound to An Inhibitor, PDB code: 2x6e 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)	20.00 / 3.35
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	83.250, 83.250, 163.310, 90.00, 90.00, 120.00
R / Rfree (%)	22.7 / 29.9

The binding sites of Bromine atom in the Aurora-A Bound to An Inhibitor (pdb code 2x6e). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Aurora-A Bound to An Inhibitor, PDB code: 2x6e:

Bromine binding site 1 out of 1 in the Aurora-A Bound to An Inhibitor


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Aurora-A Bound to An Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1389 b:0.4 occ:1.00 BR1 A:YM41389 0.0 0.4 1.0 C11 A:YM41389 1.9 99.8 1.0 C10 A:YM41389 2.9 95.3 1.0 C13 A:YM41389 2.9 93.4 1.0 N09 A:YM41389 3.1 0.4 1.0 C08 A:YM41389 3.1 0.5 1.0 C07 A:YM41389 3.8 99.4 1.0 CB A:ALA160 3.9 85.0 1.0 CD2 A:LEU194 4.2 86.7 1.0 C32 A:YM41389 4.2 89.8 1.0 N14 A:YM41389 4.2 90.0 1.0 CD1 A:LEU210 4.3 95.6 1.0 C33 A:YM41389 4.3 98.8 1.0 CG1 A:VAL147 4.4 98.7 1.0 CD1 A:LEU263 4.5 85.9 1.0 O A:GLU211 4.5 81.4 1.0 CB A:LEU210 4.6 89.8 1.0 CG2 A:VAL147 4.7 97.7 1.0 C15 A:YM41389 4.7 95.5 1.0 N06 A:YM41389 4.8 92.2 1.0

V.Bavetsias, J.M.Large, C.Sun, N.Bouloc, M.Kosmopoulou, M.Matteucci, N.E.Wilsher, V.Martins, J.Reynisson, B.Atrash, A.Faisal, F.Urban, M.Valenti, A.De Haven Brandon, G.Box, F.I.Raynaud, P.Workman, S.A.Eccles, R.Bayliss, J.Blagg, S.Linardopoulos, E.Mcdonald. Imidazo[4,5-B]Pyridine Derivatives As Inhibitors of Aurora Kinases: Lead Optimization Studies Toward the Identification of An Orally Bioavailable Preclinical Development Candidate. J. Med. Chem. V. 53 5213 2010.
ISSN: ISSN 1520-4804
PubMed: 20565112
DOI: 10.1021/JM100262J