Fluorine in PDB 3poz: Egfr Kinase Domain Complexed with Tak-285

All present enzymatic activity of Egfr Kinase Domain Complexed with Tak-285:
2.7.10.1;

The structure of Egfr Kinase Domain Complexed with Tak-285, PDB code: 3poz was solved by K.Aertgeerts, R.Skene, S.Sogabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.806, 68.881, 104.558, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 24.3

The structure of Egfr Kinase Domain Complexed with Tak-285 also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the Egfr Kinase Domain Complexed with Tak-285 (pdb code 3poz). 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 Complexed with Tak-285, PDB code: 3poz:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Egfr Kinase Domain Complexed 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 Complexed with Tak-285 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1023 b:28.7 occ:1.00 F2 A:03P1023 0.0 28.7 1.0 C22 A:03P1023 1.3 30.2 1.0 F A:03P1023 2.1 28.4 1.0 F1 A:03P1023 2.1 29.3 1.0 C20 A:03P1023 2.4 21.2 1.0 C21 A:03P1023 2.8 22.7 1.0 CB A:CYS775 3.4 23.1 1.0 C A:ARG776 3.4 23.4 1.0 OG1 A:THR790 3.5 27.2 1.0 O A:ARG776 3.5 24.6 1.0 C A:CYS775 3.6 24.4 1.0 C19 A:03P1023 3.6 24.3 1.0 N A:ARG776 3.6 25.9 1.0 N A:LEU777 3.7 24.6 1.0 O A:CYS775 3.8 25.3 1.0 OG1 A:THR854 3.8 27.0 1.0 O A:HOH14 3.9 20.7 1.0 CA A:ARG776 3.9 25.8 1.0 CB A:THR790 4.1 26.1 1.0 CA A:CYS775 4.1 22.2 1.0 C16 A:03P1023 4.2 22.1 1.0 CA A:LEU777 4.2 24.3 1.0 O A:HOH13 4.6 24.0 1.0 CG2 A:THR790 4.6 22.1 1.0 CB A:LEU777 4.8 26.6 1.0 CD1 A:LEU777 4.8 37.4 1.0 C18 A:03P1023 4.8 23.6 1.0 CE1 A:PHE856 4.8 33.5 1.0 CB A:THR854 4.8 24.6 1.0 SG A:CYS775 4.9 27.8 1.0 CZ A:PHE856 4.9 35.4 1.0 C17 A:03P1023 5.0 25.8 1.0

Fluorine binding site 2 out of 3 in the Egfr Kinase Domain Complexed 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 Complexed with Tak-285 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1023 b:28.4 occ:1.00 F A:03P1023 0.0 28.4 1.0 C22 A:03P1023 1.3 30.2 1.0 F2 A:03P1023 2.1 28.7 1.0 F1 A:03P1023 2.2 29.3 1.0 C20 A:03P1023 2.3 21.2 1.0 C19 A:03P1023 2.8 24.3 1.0 N A:LEU777 3.3 24.6 1.0 CZ A:PHE856 3.3 35.4 1.0 O A:CYS775 3.4 25.3 1.0 C21 A:03P1023 3.5 22.7 1.0 O A:MET766 3.6 27.8 1.0 C A:ARG776 3.6 23.4 1.0 CE1 A:PHE856 3.7 33.5 1.0 CA A:ARG776 3.8 25.8 1.0 C A:CYS775 3.9 24.4 1.0 CB A:MET766 4.0 26.7 1.0 CA A:LEU777 4.0 24.3 1.0 N A:ARG776 4.1 25.9 1.0 CB A:LEU777 4.1 26.6 1.0 CE2 A:PHE856 4.1 38.8 1.0 C18 A:03P1023 4.1 23.6 1.0 O A:ARG776 4.3 24.6 1.0 C A:MET766 4.3 26.4 1.0 CA A:MET766 4.4 25.2 1.0 CE A:MET766 4.5 41.1 1.0 CG A:MET766 4.6 31.8 1.0 C16 A:03P1023 4.6 22.1 1.0 CD1 A:PHE856 4.7 35.0 1.0 CB A:CYS775 4.7 23.1 1.0 CD1 A:LEU777 4.8 37.4 1.0 C17 A:03P1023 4.9 25.8 1.0 CA A:CYS775 4.9 22.2 1.0

Fluorine binding site 3 out of 3 in the Egfr Kinase Domain Complexed 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 Complexed with Tak-285 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1023 b:29.3 occ:1.00 F1 A:03P1023 0.0 29.3 1.0 C22 A:03P1023 1.3 30.2 1.0 F2 A:03P1023 2.1 28.7 1.0 F A:03P1023 2.2 28.4 1.0 C20 A:03P1023 2.3 21.2 1.0 CE1 A:PHE856 2.9 33.5 1.0 C19 A:03P1023 3.0 24.3 1.0 O A:CYS775 3.2 25.3 1.0 OG1 A:THR854 3.3 27.0 1.0 C21 A:03P1023 3.4 22.7 1.0 CZ A:PHE856 3.4 35.4 1.0 CB A:CYS775 3.4 23.1 1.0 C A:CYS775 3.5 24.4 1.0 CD1 A:PHE856 3.6 35.0 1.0 CA A:THR854 3.7 20.5 1.0 N A:ASP855 3.8 25.1 1.0 CA A:CYS775 3.9 22.2 1.0 CB A:THR854 4.0 24.6 1.0 O A:ILE853 4.1 23.6 1.0 C A:THR854 4.2 24.4 1.0 C18 A:03P1023 4.3 23.6 1.0 N A:ARG776 4.3 25.9 1.0 N A:CYS775 4.4 23.8 1.0 CE2 A:PHE856 4.4 38.8 1.0 C16 A:03P1023 4.5 22.1 1.0 CG A:PHE856 4.6 29.2 1.0 CA A:ARG776 4.7 25.8 1.0 O A:HOH14 4.8 20.7 1.0 N A:THR854 4.8 20.6 1.0 SG A:CYS775 4.8 27.8 1.0 C A:ARG776 4.9 23.4 1.0 N A:PHE856 4.9 29.9 1.0 C A:ILE853 4.9 22.5 1.0 C17 A:03P1023 4.9 25.8 1.0 CA A:ASP855 4.9 28.9 1.0 CD2 A:PHE856 5.0 33.2 1.0

K.Aertgeerts, R.Skene, J.Yano, B.C.Sang, H.Zou, G.Snell, A.Jennings, K.Iwamoto, N.Habuka, A.Hirokawa, T.Ishikawa, T.Tanaka, H.Miki, Y.Ohta, S.Sogabe. Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein. J.Biol.Chem. V. 286 18756 2011.
ISSN: ISSN 0021-9258
PubMed: 21454582
DOI: 10.1074/JBC.M110.206193