Fluorine in PDB 3w2o: Egfr Kinase Domain T790M/L858R Mutant with Tak-285

All present enzymatic activity of Egfr Kinase Domain T790M/L858R Mutant with Tak-285:
2.7.10.1;

The structure of Egfr Kinase Domain T790M/L858R Mutant with Tak-285, PDB code: 3w2o was solved by S.Sogabe, Y.Kawakita, S.Igaki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.35
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	143.953, 143.953, 143.953, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 21.6

The structure of Egfr Kinase Domain T790M/L858R Mutant with Tak-285 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Egfr Kinase Domain T790M/L858R Mutant with Tak-285 (pdb code 3w2o). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Egfr Kinase Domain T790M/L858R Mutant with Tak-285, PDB code: 3w2o:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Egfr Kinase Domain T790M/L858R Mutant with Tak-285


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Egfr Kinase Domain T790M/L858R Mutant with Tak-285 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1101 b:83.4 occ:1.00 F2 A:03P1101 0.0 83.4 1.0 C22 A:03P1101 1.3 77.2 1.0 F1 A:03P1101 2.2 75.7 1.0 F A:03P1101 2.2 79.5 1.0 C20 A:03P1101 2.4 70.0 1.0 C21 A:03P1101 2.8 66.2 1.0 NZ A:LYS745 3.4 66.6 1.0 C19 A:03P1101 3.6 66.9 1.0 CD A:LYS745 3.8 60.1 1.0 CE A:LYS745 4.1 62.0 1.0 C16 A:03P1101 4.2 62.8 1.0 CD1 A:PHE723 4.5 89.4 1.0 C18 A:03P1101 4.7 65.3 1.0 CB A:PHE723 4.8 78.7 1.0 C14 A:03P1101 4.8 52.1 1.0 C17 A:03P1101 5.0 61.6 1.0

Fluorine binding site 2 out of 3 in the Egfr Kinase Domain T790M/L858R Mutant with Tak-285


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Egfr Kinase Domain T790M/L858R Mutant with Tak-285 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1101 b:79.5 occ:1.00 F A:03P1101 0.0 79.5 1.0 C22 A:03P1101 1.3 77.2 1.0 F1 A:03P1101 2.2 75.7 1.0 F2 A:03P1101 2.2 83.4 1.0 C20 A:03P1101 2.3 70.0 1.0 C19 A:03P1101 2.7 66.9 1.0 OE2 A:GLU762 3.4 57.3 1.0 C21 A:03P1101 3.6 66.2 1.0 CG1 A:ILE759 3.9 56.5 1.0 C18 A:03P1101 4.1 65.3 1.0 CD A:GLU762 4.3 56.2 1.0 CD1 A:PHE723 4.7 89.4 1.0 CG2 A:ILE759 4.7 51.1 1.0 CB A:ILE759 4.7 55.2 1.0 C16 A:03P1101 4.8 62.8 1.0 OE1 A:GLU762 4.8 58.6 1.0 CD1 A:ILE759 4.9 58.4 1.0 CA A:ILE759 4.9 55.5 1.0 C17 A:03P1101 5.0 61.6 1.0

Fluorine binding site 3 out of 3 in the Egfr Kinase Domain T790M/L858R Mutant with Tak-285


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Egfr Kinase Domain T790M/L858R Mutant with Tak-285 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1101 b:75.7 occ:1.00 F1 A:03P1101 0.0 75.7 1.0 C22 A:03P1101 1.3 77.2 1.0 F A:03P1101 2.2 79.5 1.0 F2 A:03P1101 2.2 83.4 1.0 C20 A:03P1101 2.3 70.0 1.0 C21 A:03P1101 3.1 66.2 1.0 C19 A:03P1101 3.2 66.9 1.0 CG1 A:ILE759 3.3 56.5 1.0 CG2 A:ILE759 3.7 51.1 1.0 CD1 A:ILE759 3.8 58.4 1.0 CD2 A:LEU747 4.1 60.9 1.0 CB A:ILE759 4.1 55.2 1.0 CD A:LYS745 4.2 60.1 1.0 CB A:PHE723 4.2 78.7 1.0 C16 A:03P1101 4.4 62.8 1.0 C18 A:03P1101 4.5 65.3 1.0 NZ A:LYS745 4.5 66.6 1.0 CD1 A:PHE723 4.5 89.4 1.0 CE A:LYS745 4.6 62.0 1.0 CG A:PHE723 4.6 84.4 1.0 C17 A:03P1101 4.9 61.6 1.0 CA A:ILE759 4.9 55.5 1.0 CG A:LYS745 4.9 55.7 1.0

S.Sogabe, Y.Kawakita, S.Igaki, H.Iwata, H.Miki, D.R.Cary, T.Takagi, S.Takagi, Y.Ohta, T.Ishikawa. Structure-Based Approach For the Discovery of Pyrrolo[3,2-D]Pyrimidine-Based Egfr T790M/L858R Mutant Inhibitors. Acs Med.Chem.Lett. V. 4 201 2013.
ISSN: ISSN 1948-5875
PubMed: 24900643
DOI: 10.1021/ML300327Z