Fluorine in PDB 5cas: Egfr Kinase Domain Mutant "Tmlr" with Compound 41A

All present enzymatic activity of Egfr Kinase Domain Mutant "Tmlr" with Compound 41A:
2.7.10.1;

The structure of Egfr Kinase Domain Mutant "Tmlr" with Compound 41A, PDB code: 5cas was solved by C.Eigenbrot, C.Yu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.00 / 2.10
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	146.120, 146.120, 146.120, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 20.9

The binding sites of Fluorine atom in the Egfr Kinase Domain Mutant "Tmlr" with Compound 41A (pdb code 5cas). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Egfr Kinase Domain Mutant "Tmlr" with Compound 41A, PDB code: 5cas:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Egfr Kinase Domain Mutant "Tmlr" with Compound 41A


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 Mutant "Tmlr" with Compound 41A within 5.0Å range: probe atom residue distance (Å) B Occ A:F1102 b:58.1 occ:1.00 F15 A:4ZQ1102 0.0 58.1 1.0 C14 A:4ZQ1102 1.4 54.5 1.0 F17 A:4ZQ1102 2.2 53.2 1.0 F16 A:4ZQ1102 2.3 58.2 1.0 C12 A:4ZQ1102 2.4 51.3 1.0 N11 A:4ZQ1102 2.8 51.3 1.0 N A:GLY719 3.3 61.1 1.0 C3 A:4ZQ1102 3.4 54.1 1.0 CA A:GLY719 3.4 63.1 1.0 C A:LEU718 3.4 61.9 1.0 CB A:LEU718 3.5 52.2 1.0 C2 A:4ZQ1102 3.6 58.5 1.0 C10 A:4ZQ1102 3.7 48.5 1.0 O A:LEU718 3.7 62.2 1.0 CB A:VAL726 3.7 53.1 1.0 C13 A:4ZQ1102 3.8 47.2 1.0 CG1 A:VAL726 3.9 50.3 1.0 CA A:LEU718 4.1 55.5 1.0 CG2 A:VAL726 4.2 52.6 1.0 N4 A:4ZQ1102 4.3 51.7 1.0 C9 A:4ZQ1102 4.3 45.0 1.0 C A:GLY719 4.4 69.4 1.0 O34 A:4ZQ1102 4.4 63.6 1.0 C5 A:4ZQ1102 4.5 47.7 1.0 O A:GLY719 4.6 67.2 1.0 O A:HOH1317 4.8 90.1 1.0 CG A:LEU718 4.8 53.6 1.0 O A:VAL726 4.8 55.3 1.0 C1 A:4ZQ1102 4.8 58.2 1.0 CD1 A:LEU718 4.9 50.8 1.0 CA A:VAL726 4.9 51.2 1.0

Fluorine binding site 2 out of 4 in the Egfr Kinase Domain Mutant "Tmlr" with Compound 41A


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 Mutant "Tmlr" with Compound 41A within 5.0Å range: probe atom residue distance (Å) B Occ A:F1102 b:58.2 occ:1.00 F16 A:4ZQ1102 0.0 58.2 1.0 C14 A:4ZQ1102 1.4 54.5 1.0 F15 A:4ZQ1102 2.3 58.1 1.0 F17 A:4ZQ1102 2.3 53.2 1.0 C12 A:4ZQ1102 2.4 51.3 1.0 C13 A:4ZQ1102 2.9 47.2 1.0 N11 A:4ZQ1102 3.7 51.3 1.0 O A:HOH1317 3.8 90.1 1.0 C27 A:4ZQ1102 3.9 51.2 1.0 CG2 A:VAL726 4.3 52.6 1.0 C26 A:4ZQ1102 4.3 48.7 1.0 CA A:GLY719 4.4 63.1 1.0 C10 A:4ZQ1102 4.6 48.5 1.0 CB A:VAL726 4.6 53.1 1.0 C3 A:4ZQ1102 4.6 54.1 1.0 CZ A:PHE723 4.8 81.2 1.0 C2 A:4ZQ1102 4.8 58.5 1.0 O A:HOH1305 4.8 73.0 1.0 O A:HOH1296 4.8 74.4 1.0 N A:GLY719 4.9 61.1 1.0 C9 A:4ZQ1102 4.9 45.0 1.0 O34 A:4ZQ1102 4.9 63.6 1.0

Fluorine binding site 3 out of 4 in the Egfr Kinase Domain Mutant "Tmlr" with Compound 41A


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 Mutant "Tmlr" with Compound 41A within 5.0Å range: probe atom residue distance (Å) B Occ A:F1102 b:53.2 occ:1.00 F17 A:4ZQ1102 0.0 53.2 1.0 C14 A:4ZQ1102 1.4 54.5 1.0 F15 A:4ZQ1102 2.2 58.1 1.0 F16 A:4ZQ1102 2.3 58.2 1.0 C12 A:4ZQ1102 2.4 51.3 1.0 N11 A:4ZQ1102 3.0 51.3 1.0 C13 A:4ZQ1102 3.1 47.2 1.0 C9 A:4ZQ1102 3.1 45.0 1.0 C10 A:4ZQ1102 3.2 48.5 1.0 C27 A:4ZQ1102 3.3 51.2 1.0 C26 A:4ZQ1102 3.3 48.7 1.0 CG1 A:VAL726 3.4 50.3 1.0 CG2 A:VAL726 3.4 52.6 1.0 CB A:VAL726 3.5 53.1 1.0 N24 A:4ZQ1102 4.2 43.0 1.0 C3 A:4ZQ1102 4.2 54.1 1.0 C8 A:4ZQ1102 4.3 44.5 1.0 C5 A:4ZQ1102 4.5 47.7 1.0 N25 A:4ZQ1102 4.5 46.4 1.0 C28 A:4ZQ1102 4.9 52.8 1.0 C23 A:4ZQ1102 4.9 43.7 1.0 N4 A:4ZQ1102 4.9 51.7 1.0 N18 A:4ZQ1102 5.0 45.4 1.0

Fluorine binding site 4 out of 4 in the Egfr Kinase Domain Mutant "Tmlr" with Compound 41A


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Egfr Kinase Domain Mutant "Tmlr" with Compound 41A within 5.0Å range: probe atom residue distance (Å) B Occ A:F1102 b:51.8 occ:1.00 F31 A:4ZQ1102 0.0 51.8 1.0 C29 A:4ZQ1102 1.4 49.7 1.0 C30 A:4ZQ1102 2.3 46.1 1.0 C28 A:4ZQ1102 2.4 52.8 1.0 O32 A:4ZQ1102 2.7 56.8 1.0 N25 A:4ZQ1102 2.9 46.4 1.0 C27 A:4ZQ1102 2.9 51.2 1.0 NZ A:LYS745 3.2 55.4 1.0 CE A:LYS745 3.3 48.3 1.0 SD A:MET790 3.4 48.4 1.0 OE2 A:GLU762 3.4 58.5 1.0 C26 A:4ZQ1102 3.5 48.7 1.0 CE A:MET790 3.5 45.2 1.0 CD A:LYS745 3.6 54.7 1.0 C23 A:4ZQ1102 3.8 43.7 1.0 C33 A:4ZQ1102 4.1 59.8 1.0 O A:HOH1205 4.2 45.4 1.0 N22 A:4ZQ1102 4.3 40.6 1.0 CB A:LYS745 4.5 49.2 1.0 CD A:GLU762 4.6 71.1 1.0 N24 A:4ZQ1102 4.6 43.0 1.0 CG A:LYS745 4.7 53.3 1.0

R.Heald, K.K.Bowman, M.C.Bryan, D.Burdick, B.Chan, E.Chan, Y.Chen, S.Clausen, B.Dominguez-Fernandez, C.Eigenbrot, R.Elliott, E.J.Hanan, P.Jackson, J.Knight, H.La, M.Lainchbury, S.Malek, S.Mann, M.Merchant, K.Mortara, H.Purkey, G.Schaefer, S.Schmidt, E.Seward, S.Sideris, L.Shao, S.Wang, K.Yeap, I.Yen, C.Yu, T.P.Heffron. Noncovalent Mutant Selective Epidermal Growth Factor Receptor Inhibitors: A Lead Optimization Case Study. J.Med.Chem. V. 58 8877 2015.
ISSN: ISSN 0022-2623
PubMed: 26455919
DOI: 10.1021/ACS.JMEDCHEM.5B01412