Chlorine in PDB 4lqm: Egfr L858R in Complex with PD168393

All present enzymatic activity of Egfr L858R in Complex with PD168393:
2.7.10.1;

The structure of Egfr L858R in Complex with PD168393, PDB code: 4lqm was solved by C.H.Yun, M.J.Eck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.50
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	146.173, 146.173, 146.173, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 22.8

The structure of Egfr L858R in Complex with PD168393 also contains other interesting chemical elements:

Bromine

(Br)

1 atom

The binding sites of Chlorine atom in the Egfr L858R in Complex with PD168393 (pdb code 4lqm). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Egfr L858R in Complex with PD168393, PDB code: 4lqm:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Egfr L858R in Complex with PD168393


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Egfr L858R in Complex with PD168393 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1102 b:75.4 occ:1.00 N A:ILE878 3.5 58.6 1.0 N A:LYS879 3.6 49.2 1.0 CG A:LYS879 3.9 48.3 1.0 CB A:LYS879 4.0 49.2 1.0 CZ3 A:TRP880 4.0 41.2 1.0 O A:HOH1265 4.0 61.2 1.0 C A:PRO877 4.1 63.6 1.0 CD A:LYS879 4.1 47.2 1.0 CA A:PRO877 4.1 62.3 1.0 CA A:ILE878 4.3 57.4 1.0 CE3 A:TRP880 4.4 41.7 1.0 CB A:ILE878 4.4 58.0 1.0 O A:VAL876 4.4 73.0 1.0 CA A:LYS879 4.4 49.0 1.0 C A:ILE878 4.5 52.4 1.0 CE A:LYS879 4.8 50.9 1.0 O A:HOH1300 4.8 64.4 1.0 CG1 A:ILE878 5.0 61.1 1.0

Chlorine binding site 2 out of 2 in the Egfr L858R in Complex with PD168393


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Egfr L858R in Complex with PD168393 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1103 b:88.2 occ:1.00 NZ A:LYS913 3.5 80.1 1.0 NE A:ARG803 4.0 44.8 1.0 CZ A:ARG803 4.2 44.3 1.0 CD A:ARG803 4.4 41.6 1.0 NH2 A:ARG803 4.5 42.9 1.0 O A:GLY911 4.7 58.0 1.0 O A:HOH1237 4.7 56.0 1.0 CG A:ARG803 4.8 41.0 1.0 NH1 A:ARG803 4.8 48.0 1.0 CE A:LYS913 4.9 76.5 1.0

H.Yasuda, E.Park, C.H.Yun, N.J.Sng, A.R.Lucena-Araujo, W.L.Yeo, M.S.Huberman, D.W.Cohen, S.Nakayama, K.Ishioka, N.Yamaguchi, M.Hanna, G.R.Oxnard, C.S.Lathan, T.Moran, L.V.Sequist, J.E.Chaft, G.J.Riely, M.E.Arcila, R.A.Soo, M.Meyerson, M.J.Eck, S.S.Kobayashi, D.B.Costa. Structural, Biochemical, and Clinical Characterization of Epidermal Growth Factor Receptor (Egfr) Exon 20 Insertion Mutations in Lung Cancer. Sci Transl Med V. 5 RA177 2013.
ISSN: ISSN 1946-6234
PubMed: 24353160
DOI: 10.1126/SCITRANSLMED.3007205