Fluorine in PDB 6p1l: Crystal Structure of Egfr in Complex with EAI045

All present enzymatic activity of Crystal Structure of Egfr in Complex with EAI045:
2.7.10.1;

The structure of Crystal Structure of Egfr in Complex with EAI045, PDB code: 6p1l was solved by D.E.Heppner, M.J.Eck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	58.61 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.600, 103.150, 87.100, 90.00, 101.18, 90.00
R / Rfree (%)	20.1 / 23.7

The structure of Crystal Structure of Egfr in Complex with EAI045 also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

The binding sites of Fluorine atom in the Crystal Structure of Egfr in Complex with EAI045 (pdb code 6p1l). 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 in Complex with EAI045, PDB code: 6p1l:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Egfr in Complex with EAI045


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 in Complex with EAI045 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1103 b:44.2 occ:1.00 F06 A:9LL1103 0.0 44.2 1.0 C05 A:9LL1103 1.4 36.8 1.0 C04 A:9LL1103 2.5 31.7 1.0 C07 A:9LL1103 2.5 39.1 1.0 CE A:MET790 3.0 47.1 1.0 C A:ARG776 3.0 42.6 1.0 O A:ARG776 3.1 39.4 1.0 N A:LEU777 3.2 42.3 1.0 N A:ARG776 3.5 40.0 1.0 C A:CYS775 3.5 36.6 1.0 CB A:CYS775 3.6 32.5 1.0 O A:CYS775 3.7 39.3 1.0 CA A:ARG776 3.7 41.1 1.0 CA A:LEU777 3.7 38.1 1.0 C03 A:9LL1103 3.9 37.0 1.0 C08 A:9LL1103 3.9 33.6 1.0 SD A:MET790 4.0 43.1 1.0 CA A:CYS775 4.2 36.7 1.0 CB A:MET790 4.2 36.2 1.0 CB A:LEU777 4.3 35.7 1.0 C02 A:9LL1103 4.4 32.3 1.0 OG1 A:THR854 4.4 44.2 1.0 CG A:MET790 4.7 48.2 1.0 C10 A:9LL1103 5.0 45.8 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Egfr in Complex with EAI045


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 in Complex with EAI045 within 5.0Å range: probe atom residue distance (Å) B Occ C:F1103 b:58.3 occ:1.00 F06 C:9LL1103 0.0 58.3 1.0 C05 C:9LL1103 1.4 49.6 1.0 C07 C:9LL1103 2.5 41.0 1.0 C04 C:9LL1103 2.5 44.8 1.0 C C:ARG776 3.1 48.1 1.0 O C:ARG776 3.2 54.1 1.0 N C:LEU777 3.3 49.0 1.0 SD C:MET790 3.6 45.4 1.0 N C:ARG776 3.6 57.1 1.0 CB C:CYS775 3.6 39.5 1.0 C C:CYS775 3.6 52.8 1.0 CA C:LEU777 3.7 45.7 1.0 O C:CYS775 3.7 50.6 1.0 CA C:ARG776 3.8 46.9 1.0 C03 C:9LL1103 3.9 38.6 1.0 C08 C:9LL1103 3.9 51.6 1.0 CE C:MET790 4.0 53.3 1.0 CB C:MET790 4.1 49.8 1.0 CA C:CYS775 4.3 51.6 1.0 CB C:LEU777 4.3 42.6 1.0 OG1 C:THR854 4.4 42.7 1.0 C02 C:9LL1103 4.4 44.8 1.0 CG C:MET790 4.5 52.6 1.0 N11 C:9LL1103 5.0 42.9 1.0 C10 C:9LL1103 5.0 54.0 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Egfr in Complex with EAI045


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 in Complex with EAI045 within 5.0Å range: probe atom residue distance (Å) B Occ D:F1103 b:43.5 occ:1.00 F06 D:9LL1103 0.0 43.5 1.0 C05 D:9LL1103 1.4 34.4 1.0 C04 D:9LL1103 2.5 38.0 1.0 C07 D:9LL1103 2.5 39.3 1.0 C D:ARG776 2.9 37.6 1.0 N D:LEU777 3.0 42.2 1.0 O D:ARG776 3.0 39.9 1.0 CE D:MET790 3.2 48.2 1.0 CA D:LEU777 3.5 35.7 1.0 N D:ARG776 3.5 39.1 1.0 C D:CYS775 3.6 33.7 1.0 CA D:ARG776 3.6 33.9 1.0 O D:CYS775 3.7 31.6 1.0 CB D:CYS775 3.8 35.2 1.0 C03 D:9LL1103 3.9 35.4 1.0 C08 D:9LL1103 3.9 39.8 1.0 CB D:LEU777 4.0 37.5 1.0 SD D:MET790 4.0 35.5 1.0 CB D:MET790 4.2 39.2 1.0 CA D:CYS775 4.4 39.8 1.0 C02 D:9LL1103 4.4 37.3 1.0 CG2 D:THR854 4.5 42.0 1.0 CG D:MET790 4.7 47.4 1.0 C D:LEU777 4.8 35.7 1.0

D.J.H.De Clercq, D.E.Heppner, C.To, J.Jang, E.Park, C.H.Yun, M.Mushajiang, B.H.Shin, T.W.Gero, D.A.Scott, P.A.Janne, M.J.Eck, N.S.Gray. Discovery and Optimization of Dibenzodiazepinones As Allosteric Mutant-Selective Egfr Inhibitors. Acs Med.Chem.Lett. V. 10 1549 2019.
ISSN: ISSN 1948-5875
PubMed: 31749909
DOI: 10.1021/ACSMEDCHEMLETT.9B00381