Fluorine in PDB 5dn3: Aurora A in Complex with Atp and AA35.

All present enzymatic activity of Aurora A in Complex with Atp and AA35.:
2.7.11.1;

The structure of Aurora A in Complex with Atp and AA35., PDB code: 5dn3 was solved by M.Janecek, M.Rossmann, P.Sharma, A.Emery, G.Mckenzie, D.Huggins, S.Stockwell, J.A.Stokes, E.G.Almeida, B.Hardwick, A.J.Narvaez, M.Hyvonen, D.R.Spring, A.Venkitaraman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.91 / 2.05
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.650, 81.650, 136.910, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 20.3

The structure of Aurora A in Complex with Atp and AA35. also contains other interesting chemical elements:

Magnesium	(Mg)	1 atom
Bromine	(Br)	1 atom

The binding sites of Fluorine atom in the Aurora A in Complex with Atp and AA35. (pdb code 5dn3). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Aurora A in Complex with Atp and AA35., PDB code: 5dn3:

Fluorine binding site 1 out of 1 in the Aurora A in Complex with Atp and AA35.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Aurora A in Complex with Atp and AA35. within 5.0Å range: probe atom residue distance (Å) B Occ A:F402 b:54.7 occ:1.00 F17 A:5DN402 0.0 54.7 1.0 C16 A:5DN402 1.4 54.6 1.0 C18 A:5DN402 2.3 54.6 1.0 C15 A:5DN402 2.4 58.3 1.0 N14 A:5DN402 2.7 62.1 1.0 CD1 A:LEU169 3.3 35.1 1.0 CG A:GLU175 3.6 42.6 1.0 C19 A:5DN402 3.7 56.7 1.0 C21 A:5DN402 3.7 60.5 1.0 CB A:LEU169 3.8 30.4 1.0 CD2 A:LEU178 3.9 42.6 1.0 C06 A:5DN402 4.1 67.2 1.0 CG A:LEU169 4.1 35.2 1.0 O A:HOH620 4.2 56.7 1.0 C20 A:5DN402 4.2 59.1 1.0 CB A:GLU175 4.3 35.0 1.0 CA A:GLU175 4.5 33.3 1.0 CG2 A:VAL206 4.5 36.2 1.0 C13 A:5DN402 4.7 79.4 1.0 CG A:LYS166 4.8 40.3 1.0 CD A:GLU175 4.9 56.5 1.0 C04 A:5DN402 4.9 64.5 1.0 C07 A:5DN402 5.0 74.4 1.0 CD2 A:LEU169 5.0 35.2 1.0

M.Janecek, M.Rossmann, P.Sharma, A.Emery, D.J.Huggins, S.R.Stockwell, J.E.Stokes, Y.S.Tan, E.G.Almeida, B.Hardwick, A.J.Narvaez, M.Hyvonen, D.R.Spring, G.J.Mckenzie, A.R.Venkitaraman. Allosteric Modulation of Aurka Kinase Activity By A Small-Molecule Inhibitor of Its Protein-Protein Interaction with TPX2. Sci Rep V. 6 28528 2016.
ISSN: ESSN 2045-2322
PubMed: 27339427
DOI: 10.1038/SREP28528