Fluorine in PDB 5ory: Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment

All present enzymatic activity of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment:
2.7.11.1;

The structure of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment, PDB code: 5ory was solved by P.J.Mcintyre, P.M.Collins, F.Von Delft, R.Bayliss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	71.14 / 1.99
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	82.140, 82.140, 176.250, 90.00, 90.00, 120.00
R / Rfree (%)	20.4 / 26.5

The structure of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Chlorine	(Cl)	3 atoms

The binding sites of Fluorine atom in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment (pdb code 5ory). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment, PDB code: 5ory:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:F406 b:0.5 occ:1.00 F1 A:AY4406 0.0 0.5 1.0 C8 A:AY4406 1.4 0.9 1.0 C7 A:AY4406 2.4 0.8 1.0 C9 A:AY4406 2.4 0.8 1.0 O1 A:AY4406 2.7 0.3 1.0 CD2 A:HIS201 3.0 94.4 1.0 CE2 A:TYR199 3.0 86.0 1.0 CD2 A:TYR199 3.3 71.1 1.0 C6 A:AY4406 3.6 0.2 1.0 NE2 A:HIS201 3.6 96.7 1.0 C4 A:AY4406 3.7 0.1 1.0 CZ A:TYR199 4.1 82.0 1.0 C5 A:AY4406 4.1 0.5 1.0 CG A:HIS201 4.1 94.3 1.0 OH A:TYR199 4.5 91.7 1.0 CG A:TYR199 4.6 59.2 1.0 F2 A:AY4406 4.7 0.7 1.0 CB A:HIS201 4.8 83.8 1.0 CE1 A:HIS201 4.9 98.5 1.0 C3 A:AY4406 4.9 0.7 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Aurora-A Kinase in Complex with An Allosterically Binding Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:F406 b:0.7 occ:1.00 F2 A:AY4406 0.0 0.7 1.0 C6 A:AY4406 1.4 0.2 1.0 C5 A:AY4406 2.4 0.5 1.0 C7 A:AY4406 2.4 0.8 1.0 CG2 A:VAL182 3.5 59.6 1.0 CG A:ARG179 3.5 73.4 1.0 CA A:ARG179 3.5 49.6 1.0 C8 A:AY4406 3.6 0.9 1.0 C4 A:AY4406 3.6 0.1 1.0 CB A:VAL182 3.9 55.8 1.0 O A:HOH559 3.9 71.0 1.0 O A:LEU178 3.9 52.6 1.0 N A:ARG179 4.0 47.9 1.0 C9 A:AY4406 4.1 0.8 1.0 CB A:ARG179 4.1 57.4 1.0 C A:LEU178 4.1 52.6 1.0 CG A:LEU178 4.4 60.0 1.0 CG1 A:VAL182 4.4 58.0 1.0 C A:ARG179 4.6 52.5 1.0 O A:ARG179 4.7 54.2 1.0 F1 A:AY4406 4.7 0.5 1.0 CD2 A:LEU178 4.7 62.7 1.0 C3 A:AY4406 4.8 0.7 1.0 CD A:ARG179 4.9 78.5 1.0 NH1 A:ARG179 4.9 98.3 1.0 CB A:LEU178 5.0 52.3 1.0

P.J.Mcintyre, P.M.Collins, L.Vrzal, K.Birchall, L.H.Arnold, C.Mpamhanga, P.J.Coombs, S.G.Burgess, M.W.Richards, A.Winter, V.Veverka, F.V.Delft, A.Merritt, R.Bayliss. Characterization of Three Druggable Hot-Spots in the Aurora-A/TPX2 Interaction Using Biochemical, Biophysical, and Fragment-Based Approaches. Acs Chem. Biol. V. 12 2906 2017.
ISSN: ESSN 1554-8937
PubMed: 29045126
DOI: 10.1021/ACSCHEMBIO.7B00537