Bromine in PDB 2qlq: Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3

All present enzymatic activity of Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3:
2.7.10.2;

The structure of Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3, PDB code: 2qlq was solved by A.Michalczyk, H.B.Rode, C.Gruetter, D.Rauh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.93 / 2.33
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	41.940, 63.530, 74.500, 78.28, 90.37, 89.45
R / Rfree (%)	21.2 / 26.7

The binding sites of Bromine atom in the Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3 (pdb code 2qlq). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 3 binding sites of Bromine where determined in the Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3, PDB code: 2qlq:
Jump to Bromine binding site number: 1; 2; 3;

Bromine binding site 1 out of 3 in the Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1345 b:51.5 occ:0.70 BRR1 A:SR21345 0.0 51.5 0.7 C3 A:SR21345 1.9 46.0 0.7 C21 A:SR21345 2.0 45.5 0.3 C22 A:SR21345 2.3 43.3 0.3 C22 A:SR21345 2.9 43.3 0.7 C4 A:SR21345 3.0 43.5 0.7 O A:HOH96 3.2 47.9 1.0 C20 A:SR21345 3.4 44.2 0.3 SD A:MET314 3.5 43.6 1.0 OD2 A:ASP404 3.5 41.6 1.0 N A:ASP404 3.6 33.8 1.0 C3 A:SR21345 3.6 46.0 0.3 CA A:ASP404 3.9 36.3 1.0 C21 A:SR21345 4.2 45.5 0.7 CG A:ASP404 4.2 40.3 1.0 C5 A:SR21345 4.3 43.0 0.7 CE A:MET314 4.4 41.1 1.0 CG1 A:VAL323 4.4 28.1 1.0 C5 A:SR21345 4.5 43.0 0.3 C4 A:SR21345 4.6 43.5 0.3 CB A:ASP404 4.7 37.1 1.0 C A:ALA403 4.7 31.8 1.0 C20 A:SR21345 4.7 44.2 0.7 CG A:MET314 4.8 41.9 1.0 BRR1 A:SR21345 4.8 51.5 0.3 CB A:ALA403 4.9 29.6 1.0 CD A:LYS295 4.9 52.2 1.0 CA A:ALA403 4.9 30.1 1.0

Bromine binding site 2 out of 3 in the Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1345 b:51.5 occ:0.30 BRR1 A:SR21345 0.0 51.5 0.3 C21 A:SR21345 1.0 45.5 0.7 C3 A:SR21345 1.8 46.0 0.3 C22 A:SR21345 2.0 43.3 0.7 C20 A:SR21345 2.1 44.2 0.7 C4 A:SR21345 2.7 43.5 0.3 C22 A:SR21345 2.8 43.3 0.3 O A:ILE336 3.1 45.1 1.0 CB A:LYS295 3.1 51.6 1.0 N A:LYS295 3.2 50.1 1.0 C3 A:SR21345 3.3 46.0 0.7 C5 A:SR21345 3.4 43.0 0.7 CA A:LYS295 3.7 51.7 1.0 CG2 A:THR338 3.7 20.0 1.0 C4 A:SR21345 3.7 43.5 0.7 C A:ILE336 3.9 45.1 1.0 C5 A:SR21345 3.9 43.0 0.3 C A:ILE294 4.0 48.8 1.0 OG1 A:THR338 4.0 20.0 1.0 C21 A:SR21345 4.0 45.5 0.3 CG2 A:ILE336 4.1 47.0 1.0 CB A:ILE336 4.2 47.0 1.0 O A:ALA293 4.2 45.1 1.0 CA A:ILE294 4.3 47.8 1.0 CG A:LYS295 4.3 52.0 1.0 CD A:LYS295 4.4 52.2 1.0 C20 A:SR21345 4.4 44.2 0.3 CB A:THR338 4.5 20.0 1.0 C A:ALA293 4.5 45.8 1.0 N A:ILE294 4.5 46.8 1.0 N1 A:SR21345 4.5 35.8 0.7 CA A:ILE336 4.6 47.0 1.0 N A:THR338 4.6 20.0 1.0 N A:VAL337 4.7 42.8 1.0 BRR1 A:SR21345 4.8 51.5 0.7 O A:ILE294 4.9 49.3 1.0 CA A:VAL337 4.9 40.9 1.0 C A:VAL337 4.9 39.6 1.0 C A:LYS295 4.9 52.6 1.0 N1 A:SR21345 4.9 35.8 0.3 N3 A:SR21345 4.9 28.7 0.7 CB A:ALA293 4.9 45.4 1.0

Bromine binding site 3 out of 3 in the Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Src Kinase Domain with Covalent Inhibitor RL3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1345 b:74.7 occ:0.60 BRR1 B:SR21345 0.0 74.7 0.6 C3 B:SR21345 1.9 72.8 0.6 C4 B:SR21345 2.9 71.5 0.6 C22 B:SR21345 2.9 71.3 0.6 O B:ILE336 3.3 33.3 1.0 N B:LYS295 3.5 42.0 1.0 OG1 B:THR338 3.6 31.5 1.0 CB B:LYS295 3.6 44.5 1.0 O B:ALA293 3.8 34.9 1.0 C B:ILE336 3.9 33.2 1.0 CG2 B:THR338 4.0 31.6 1.0 C B:ALA293 4.0 36.3 1.0 C B:ILE294 4.1 40.0 1.0 CB B:ILE336 4.1 34.4 1.0 CA B:LYS295 4.1 44.5 1.0 N B:ILE294 4.2 36.8 1.0 CA B:ILE294 4.2 38.2 1.0 C21 B:SR21345 4.2 72.9 0.6 C5 B:SR21345 4.2 71.0 0.6 CG2 B:ILE336 4.2 33.8 1.0 N B:THR338 4.3 30.9 1.0 CB B:THR338 4.4 31.0 1.0 N B:VAL337 4.4 31.8 1.0 CB B:ALA293 4.4 36.0 1.0 CA B:VAL337 4.6 31.3 1.0 C B:VAL337 4.7 31.0 1.0 CA B:ILE336 4.7 34.0 1.0 C20 B:SR21345 4.7 72.0 0.6 CG B:LYS295 4.9 44.8 1.0 O B:ILE294 4.9 40.4 1.0 CA B:ALA293 4.9 36.8 1.0 CA B:THR338 5.0 31.1 1.0

A.Michalczyk, S.Kluter, H.B.Rode, J.R.Simard, C.Grutter, M.Rabiller, D.Rauh. Structural Insights Into How Irreversible Inhibitors Can Overcome Drug Resistance in Egfr. Bioorg.Med.Chem. V. 16 3482 2008.
ISSN: ISSN 0968-0896
PubMed: 18316192
DOI: 10.1016/J.BMC.2008.02.053