Fluorine in PDB 5uwd: Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686

All present enzymatic activity of Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686:
2.7.10.1;

The structure of Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686, PDB code: 5uwd was solved by K.S.Gajiwala, R.A.Ferre, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.35 / 3.06
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.926, 78.926, 215.596, 90.00, 90.00, 120.00
R / Rfree (%)	21.3 / 28

The binding sites of Fluorine atom in the Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686 (pdb code 5uwd). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686, PDB code: 5uwd:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686


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 Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686 within 5.0Å range: probe atom residue distance (Å) B Occ A:F9001 b:73.0 occ:1.00 F8 A:8OV9001 0.0 73.0 1.0 C7 A:8OV9001 1.4 74.5 1.0 F9 A:8OV9001 2.2 71.0 1.0 F10 A:8OV9001 2.3 74.2 1.0 C5 A:8OV9001 2.4 78.9 1.0 C6 A:8OV9001 2.7 79.4 1.0 CG A:MET790 3.0 91.8 1.0 CB A:MET790 3.5 88.2 1.0 C4 A:8OV9001 3.7 80.6 1.0 SG A:CYS775 3.9 0.2 1.0 CD1 A:LEU844 4.0 77.0 1.0 N1 A:8OV9001 4.1 80.6 1.0 O A:GLN791 4.1 90.5 1.0 OG1 A:THR854 4.2 94.5 1.0 SD A:MET790 4.3 95.4 1.0 N11 A:8OV9001 4.3 79.8 1.0 CZ A:PHE856 4.3 0.9 1.0 CE2 A:PHE856 4.4 0.6 1.0 CB A:ALA743 4.5 82.5 1.0 CE A:MET790 4.5 92.3 1.0 N3 A:8OV9001 4.7 82.3 1.0 CB A:CYS775 4.8 0.0 1.0 CA A:MET790 4.9 86.2 1.0 C2 A:8OV9001 4.9 84.1 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686


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 Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686 within 5.0Å range: probe atom residue distance (Å) B Occ A:F9001 b:71.0 occ:1.00 F9 A:8OV9001 0.0 71.0 1.0 C7 A:8OV9001 1.4 74.5 1.0 F8 A:8OV9001 2.2 73.0 1.0 F10 A:8OV9001 2.2 74.2 1.0 C5 A:8OV9001 2.4 78.9 1.0 C4 A:8OV9001 3.3 80.6 1.0 C6 A:8OV9001 3.4 79.4 1.0 N11 A:8OV9001 3.5 79.8 1.0 CB A:ALA743 3.5 82.5 1.0 CB A:MET790 3.6 88.2 1.0 CG1 A:VAL726 3.8 85.5 1.0 CG A:MET790 3.8 91.8 1.0 NZ A:LYS745 4.1 0.8 1.0 CE A:MET790 4.2 92.3 1.0 N3 A:8OV9001 4.5 82.3 1.0 CG2 A:VAL726 4.5 85.5 1.0 CZ A:PHE856 4.6 0.9 1.0 N1 A:8OV9001 4.6 80.6 1.0 CD A:LYS745 4.6 96.0 1.0 C A:ALA743 4.6 85.2 1.0 CA A:ALA743 4.7 82.0 1.0 CB A:LYS745 4.7 84.2 1.0 CG A:LYS745 4.7 89.5 1.0 CE2 A:PHE856 4.8 0.6 1.0 CB A:VAL726 4.8 86.0 1.0 O A:ALA743 4.8 85.2 1.0 SD A:MET790 4.8 95.4 1.0 C12 A:8OV9001 4.9 78.7 1.0 CE A:LYS745 5.0 0.5 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Egfr Kinase Domain (L858R, T790M, V948R) in Complex with the Covalent Inhibitor Co-1686 within 5.0Å range: probe atom residue distance (Å) B Occ A:F9001 b:74.2 occ:1.00 F10 A:8OV9001 0.0 74.2 1.0 C7 A:8OV9001 1.4 74.5 1.0 F9 A:8OV9001 2.2 71.0 1.0 F8 A:8OV9001 2.3 73.0 1.0 C5 A:8OV9001 2.4 78.9 1.0 N11 A:8OV9001 2.7 79.8 1.0 C4 A:8OV9001 2.9 80.6 1.0 NZ A:LYS745 3.3 0.8 1.0 CE2 A:PHE856 3.5 0.6 1.0 C6 A:8OV9001 3.7 79.4 1.0 CD1 A:LEU844 3.8 77.0 1.0 OG1 A:THR854 3.9 94.5 1.0 C12 A:8OV9001 3.9 78.7 1.0 CZ A:PHE856 4.0 0.9 1.0 N3 A:8OV9001 4.2 82.3 1.0 C17 A:8OV9001 4.3 80.1 1.0 CE A:LYS745 4.6 0.5 1.0 CD2 A:PHE856 4.7 0.5 1.0 N1 A:8OV9001 4.8 80.6 1.0 CD A:LYS745 4.9 96.0 1.0 CG A:MET790 4.9 91.8 1.0 CG2 A:VAL726 4.9 85.5 1.0 CG1 A:VAL726 5.0 85.5 1.0 C2 A:8OV9001 5.0 84.1 1.0

S.Niessen, M.M.Dix, S.Barbas, Z.E.Potter, S.Lu, O.Brodsky, S.Planken, D.Behenna, C.Almaden, K.S.Gajiwala, K.Ryan, R.Ferre, M.R.Lazear, M.M.Hayward, J.C.Kath, B.F.Cravatt. Proteome-Wide Map of Targets of T790M-Egfr-Directed Covalent Inhibitors. Cell Chem Biol V. 24 1388 2017.
ISSN: ESSN 2451-9456
PubMed: 28965727
DOI: 10.1016/J.CHEMBIOL.2017.08.017