Fluorine in PDB 8d76: Crystal Structure of Egfr Lrtm with Compound 24

All present enzymatic activity of Crystal Structure of Egfr Lrtm with Compound 24:
2.7.10.1;

The structure of Crystal Structure of Egfr Lrtm with Compound 24, PDB code: 8d76 was solved by J.L.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.40
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	41.535, 50.316, 85.875, 104.19, 101.73, 90.12
R / Rfree (%)	15.6 / 26

The binding sites of Fluorine atom in the Crystal Structure of Egfr Lrtm with Compound 24 (pdb code 8d76). 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 Egfr Lrtm with Compound 24, PDB code: 8d76:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Egfr Lrtm with Compound 24


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 Lrtm with Compound 24 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1504 b:52.9 occ:1.00 F1 A:QFO1504 0.0 52.9 1.0 C22 A:QFO1504 1.4 54.0 1.0 C21 A:QFO1504 2.4 56.2 1.0 C24 A:QFO1504 2.4 50.9 1.0 C23 A:QFO1504 2.4 51.5 1.0 C20 A:QFO1504 2.8 56.4 1.0 O3 A:QFO1504 2.9 52.2 1.0 N7 A:QFO1504 2.9 47.8 1.0 CG2 A:VAL726 3.0 72.6 1.0 CD A:LYS745 3.2 56.2 1.0 C19 A:QFO1504 3.4 53.0 1.0 CG A:LYS745 3.6 58.7 1.0 CE A:MET790 3.7 57.7 1.0 C16 A:QFO1504 3.8 44.3 1.0 CE A:LYS745 3.9 55.8 1.0 CB A:LYS745 3.9 51.4 1.0 N5 A:QFO1504 4.1 40.1 1.0 NZ A:LYS745 4.4 57.6 1.0 CB A:VAL726 4.4 65.9 1.0 SD A:MET790 4.4 52.7 1.0 CD1 A:PHE723 4.6 53.1 1.0 CG1 A:VAL726 4.7 67.2 1.0 N6 A:QFO1504 4.8 47.8 1.0 CA A:LYS745 4.9 48.4 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Egfr Lrtm with Compound 24


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 Lrtm with Compound 24 within 5.0Å range: probe atom residue distance (Å) B Occ B:F1503 b:56.5 occ:1.00 F1 B:QFO1503 0.0 56.5 1.0 C22 B:QFO1503 1.4 43.8 1.0 C23 B:QFO1503 2.4 54.4 1.0 C24 B:QFO1503 2.4 51.7 1.0 C21 B:QFO1503 2.4 57.5 1.0 O3 B:QFO1503 2.8 51.1 1.0 C20 B:QFO1503 2.9 58.0 1.0 CG2 B:VAL726 2.9 62.9 0.5 N7 B:QFO1503 2.9 50.8 1.0 C19 B:QFO1503 3.4 58.0 1.0 CD B:LYS745 3.5 62.6 1.0 C16 B:QFO1503 3.7 43.8 1.0 CE B:MET790 3.7 53.1 1.0 CG B:LYS745 3.9 63.0 1.0 N5 B:QFO1503 4.0 41.7 1.0 CE B:LYS745 4.1 67.7 1.0 CB B:LYS745 4.1 53.0 1.0 CB B:VAL726 4.2 53.9 0.5 CG2 B:VAL726 4.2 51.1 0.5 CB B:VAL726 4.3 61.1 0.5 NZ B:LYS745 4.4 66.8 1.0 SD B:MET790 4.5 52.1 1.0 CD1 B:PHE723 4.5 58.8 1.0 CG1 B:VAL726 4.6 56.4 0.5 CG1 B:VAL726 4.8 47.9 0.5 N6 B:QFO1503 4.8 47.1 1.0 CE1 B:PHE723 4.9 52.0 1.0 C2 B:QFO1503 4.9 48.9 1.0

M.S.Eno, J.D.Brubaker, J.E.Campbell, C.De Savi, T.J.Guzi, B.D.Williams, D.Wilson, K.Wilson, N.Brooijmans, J.Kim, A.Ozen, E.Perola, J.Hsieh, V.Brown, K.Fetalvero, A.Garner, Z.Zhang, F.Stevison, R.Woessner, J.Singh, Y.Timsit, C.Kinkema, C.Medendorp, C.Lee, F.Albayya, A.Zalutskaya, S.Schalm, T.A.Dineen. Discovery of Blu-945, A Reversible, Potent, and Wild-Type-Sparing Next-Generation Egfr Mutant Inhibitor For Treatment-Resistant Non-Small-Cell Lung Cancer. J.Med.Chem. V. 65 9662 2022.
ISSN: ISSN 0022-2623
PubMed: 35838760
DOI: 10.1021/ACS.JMEDCHEM.2C00704