Chlorine in PDB 2zva: Lyn Tyrosine Kinase Domain-Dasatinib Complex

All present enzymatic activity of Lyn Tyrosine Kinase Domain-Dasatinib Complex:
2.7.10.2;

The structure of Lyn Tyrosine Kinase Domain-Dasatinib Complex, PDB code: 2zva was solved by N.K.Williams, J.Rossjohn, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.37 / 2.60
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	127.378, 127.378, 55.619, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / 23.1

The binding sites of Chlorine atom in the Lyn Tyrosine Kinase Domain-Dasatinib Complex (pdb code 2zva). 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 Lyn Tyrosine Kinase Domain-Dasatinib Complex, PDB code: 2zva:

Chlorine binding site 1 out of 1 in the Lyn Tyrosine Kinase Domain-Dasatinib Complex


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Lyn Tyrosine Kinase Domain-Dasatinib Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl513 b:48.1 occ:1.00 CL A:1N1513 0.0 48.1 1.0 C5 A:1N1513 1.8 45.7 1.0 C6 A:1N1513 2.8 44.1 1.0 C4 A:1N1513 2.8 46.6 1.0 N2 A:1N1513 3.0 49.0 1.0 CB A:ALA384 3.4 23.6 1.0 N A:ASP385 3.6 27.4 1.0 CG1 A:VAL303 3.6 17.9 1.0 CA A:ALA384 3.6 24.9 1.0 C3 A:1N1513 3.6 50.1 1.0 CB A:VAL303 3.7 19.7 1.0 O A:1N1513 3.9 48.6 1.0 C7 A:1N1513 4.1 46.2 1.0 C9 A:1N1513 4.1 46.9 1.0 C A:ALA384 4.1 26.6 1.0 CG2 A:VAL303 4.1 18.8 1.0 CD1 A:LEU374 4.4 13.1 1.0 CE2 A:PHE386 4.5 16.7 1.0 C8 A:1N1513 4.6 47.6 1.0 C2 A:1N1513 4.6 49.2 1.0 CA A:ASP385 4.7 28.8 1.0 CD2 A:PHE386 4.8 17.9 1.0 SD A:MET294 4.9 26.6 1.0 OG1 A:THR319 4.9 24.2 1.0 N A:ALA384 4.9 24.1 1.0 O A:ILE383 5.0 24.2 1.0

N.K.Williams, I.S.Lucet, S.P.Klinken, E.Ingley, J.Rossjohn. Crystal Structures of the Lyn Protein Tyrosine Kinase Domain in Its Apo- and Inhibitor-Bound State J.Biol.Chem. V. 284 284 2009.
ISSN: ISSN 0021-9258
PubMed: 18984583
DOI: 10.1074/JBC.M807850200