Fluorine in PDB 5byz: ERK5 in Complex with Small Molecule

All present enzymatic activity of ERK5 in Complex with Small Molecule:
2.7.11.24;

The structure of ERK5 in Complex with Small Molecule, PDB code: 5byz was solved by H.Chen, J.Tucker, X.Wang, P.R.Gavine, C.Philips, M.A.Augustin, P.Schreiner, S.Steinbacher, M.Preston, D.Ogg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.82 / 1.65
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	93.401, 93.401, 116.280, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 19.2

The binding sites of Fluorine atom in the ERK5 in Complex with Small Molecule (pdb code 5byz). 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 ERK5 in Complex with Small Molecule, PDB code: 5byz:

Fluorine binding site 1 out of 1 in the ERK5 in Complex with Small Molecule


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of ERK5 in Complex with Small Molecule within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:22.5 occ:1.00 F16 A:4WE401 0.0 22.5 1.0 C15 A:4WE401 1.3 20.8 1.0 C14 A:4WE401 2.4 19.4 1.0 C10 A:4WE401 2.4 20.2 1.0 C8 A:4WE401 2.9 22.3 1.0 C9 A:4WE401 2.9 18.9 1.0 CB A:LEU137 3.4 22.5 1.0 CG1 A:ILE115 3.4 21.6 1.0 CD2 A:LEU137 3.5 22.7 1.0 CD1 A:LEU137 3.5 21.1 1.0 N13 A:4WE401 3.6 20.5 1.0 CG A:LEU137 3.6 22.9 1.0 N11 A:4WE401 3.6 20.4 1.0 CD1 A:ILE115 3.6 23.0 1.0 C12 A:4WE401 4.0 21.3 1.0 N7 A:4WE401 4.2 22.9 1.0 O A:ASP138 4.2 21.6 1.0 N4 A:4WE401 4.3 20.2 1.0 CD1 A:LEU189 4.3 20.6 1.0 CB A:ALA82 4.6 22.0 1.0 CB A:ILE115 4.7 20.5 1.0 CA A:LEU137 4.8 22.3 1.0 C5 A:4WE401 4.8 21.3 1.0 O A:HOH696 4.9 19.7 1.0 CG2 A:ILE115 5.0 21.0 1.0

H.Chen, J.Tucker, X.Wang, P.R.Gavine, C.Phillips, M.A.Augustin, P.Schreiner, S.Steinbacher, M.Preston, D.Ogg. Discovery of A Novel Allosteric Inhibitor-Binding Site in ERK5: Comparison with the Canonical Kinase Hinge Atp-Binding Site. Acta Crystallogr D Struct V. 72 682 2016BIOL.
ISSN: ISSN 2059-7983
PubMed: 27139631
DOI: 10.1107/S2059798316004502