Chlorine in PDB 4wd5: Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138

All present enzymatic activity of Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138:
2.7.10.1;

The structure of Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138, PDB code: 4wd5 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)	37.64 / 3.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.575, 93.288, 163.860, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 23.9

The binding sites of Chlorine atom in the Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138 (pdb code 4wd5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138, PDB code: 4wd5:

Chlorine binding site 1 out of 1 in the Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1101 b:93.9 occ:1.00 N B:ILE878 3.2 72.5 1.0 CA B:PRO877 3.4 72.3 1.0 O B:VAL876 3.6 82.3 1.0 C B:PRO877 3.7 71.9 1.0 N B:LYS879 3.9 57.9 1.0 CG B:LYS879 4.2 80.2 1.0 CA B:ILE878 4.2 70.2 1.0 N B:PRO877 4.3 77.3 1.0 C B:VAL876 4.4 82.2 1.0 CB B:ILE878 4.4 67.7 1.0 CZ3 B:TRP880 4.4 55.7 1.0 CB B:PRO877 4.6 70.3 1.0 C B:ILE878 4.6 64.9 1.0 CB B:LYS879 4.6 74.0 1.0 CE3 B:TRP880 4.6 56.5 1.0 O B:PRO877 4.8 71.8 1.0 CA B:LYS879 4.9 66.4 1.0 CE B:LYS879 5.0 97.1 1.0

H.Wu, C.Hu, A.Wang, E.E.Weisberg, Y.Chen, C.H.Yun, W.Wang, X.Liu, B.Tian, J.Wang, Z.Zhao, Y.Liang, B.Li, L.Wang, B.Wang, C.Chen, S.J.Buhrlage, S.M.Fernadners, J.Griffin, J.R.Brown, M.J.Eck, J.Liu, Q.Liu, N.S.Gray. Crystal Structure of Egfr 696-1022 T790M in Complex with Ql-X138 To Be Published.