Chlorine in PDB 7uy0: Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259

All present enzymatic activity of Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259:
2.7.10.2;

The structure of Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259, PDB code: 7uy0 was solved by S.Du, J.J.Alvarado, T.E.Smithgall, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	77.35 / 2.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.43, 112.09, 213.73, 90, 90, 90
R / Rfree (%)	18.7 / 22.3

The binding sites of Chlorine atom in the Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259 (pdb code 7uy0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259, PDB code: 7uy0:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259


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 Human Fgr Tyrosine Kinase in Complex with A- 419259 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl604 b:83.5 occ:1.00 NH2 A:ARG95 3.4 52.8 1.0 OG1 A:THR252 3.4 64.9 1.0 N A:THR252 3.4 69.3 1.0 OH A:TYR326 3.5 71.1 1.0 CB A:GLN251 3.8 80.4 1.0 CA A:GLN251 3.9 75.3 1.0 CZ A:TYR326 4.0 63.5 1.0 NH1 A:ARG95 4.1 52.7 1.0 CZ A:ARG95 4.1 53.6 1.0 CG A:GLN251 4.1 87.1 1.0 C A:GLN251 4.2 71.6 1.0 O A:THR252 4.2 65.5 1.0 CB A:THR252 4.3 63.2 1.0 CA A:THR252 4.4 64.7 1.0 CE1 A:TYR326 4.4 57.7 1.0 CD A:GLN251 4.5 95.5 1.0 CG2 A:THR252 4.7 63.2 1.0 C A:THR252 4.7 66.2 1.0 CE2 A:TYR326 4.8 59.7 1.0 OE1 A:GLN251 4.9 95.1 1.0 NE2 A:GLN251 4.9 100.3 1.0 CG2 A:THR290 4.9 48.6 1.0 O A:HOH715 4.9 63.9 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl603 b:71.9 occ:1.00 N B:LYS427 3.2 46.7 1.0 N B:ILE426 3.3 54.4 1.0 CG B:LYS427 3.4 48.2 1.0 CE B:LYS468 3.5 70.4 1.0 CB B:LYS427 3.6 50.0 1.0 C B:PRO425 3.8 56.6 1.0 CZ3 B:TRP428 3.8 45.9 1.0 CA B:PRO425 3.9 60.5 1.0 CG B:LYS468 3.9 63.7 1.0 O B:PHE424 3.9 75.1 1.0 CA B:LYS427 4.0 53.1 1.0 CD B:LYS427 4.0 52.4 1.0 CE3 B:TRP428 4.0 46.0 1.0 CA B:ILE426 4.1 52.2 1.0 CD B:LYS468 4.1 68.8 1.0 C B:ILE426 4.1 51.4 1.0 CB B:ILE426 4.2 52.8 1.0 NZ B:LYS468 4.5 73.1 1.0 O B:PRO425 4.6 56.6 1.0 CE B:LYS427 4.7 60.0 1.0 C B:PHE424 4.8 77.0 1.0 N B:PRO425 4.9 65.8 1.0 CB B:PRO425 5.0 58.5 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl604 b:96.3 occ:1.00 O B:GLU178 3.5 81.8 1.0 N B:LYS181 3.8 81.9 1.0 CB B:LYS181 3.8 86.2 1.0 CA B:LYS181 3.8 83.5 1.0 O B:SER177 3.9 77.1 1.0 C B:GLU178 4.2 78.7 1.0 C B:THR180 4.4 81.4 1.0 CG B:LYS181 4.5 89.7 1.0 N B:THR180 4.6 81.4 1.0 C B:THR179 4.7 82.3 1.0 N B:THR179 4.8 78.5 1.0 CA B:GLU178 4.9 75.6 1.0 O B:THR180 4.9 79.1 1.0 O B:THR179 4.9 85.0 1.0 CA B:THR180 5.0 82.1 1.0 C B:SER177 5.0 73.1 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Human Fgr Tyrosine Kinase in Complex with A- 419259 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl605 b:93.2 occ:1.00 NH2 B:ARG95 3.3 74.1 1.0 CB B:GLN251 3.3 104.8 1.0 OH B:TYR326 3.4 81.2 1.0 N B:THR252 3.5 98.0 1.0 CA B:GLN251 3.7 100.0 1.0 OG1 B:THR252 3.8 97.2 1.0 CG B:GLN251 3.9 105.8 1.0 CZ B:TYR326 4.0 82.2 1.0 CZ B:ARG95 4.1 76.1 1.0 C B:GLN251 4.1 97.8 1.0 NH1 B:ARG95 4.2 75.6 1.0 O B:THR252 4.4 108.5 1.0 CE1 B:TYR326 4.4 82.4 1.0 CA B:THR252 4.5 101.8 1.0 CB B:THR252 4.5 98.1 1.0 CD B:GLN251 4.6 107.5 1.0 OE1 B:GLN251 4.7 109.2 1.0 CG2 B:THR252 4.7 96.6 1.0 CE2 B:TYR326 4.8 80.3 1.0 C B:THR252 4.9 109.3 1.0

S.Du, J.J.Alvarado, T.E.Wales, J.A.Moroco, J.R.Engen, T.E.Smithgall. Atp-Site Inhibitors Induce Unique Conformations of the Acute Myeloid Leukemia-Associated Src-Family Kinase, Fgr. Structure V. 30 1508 2022.
ISSN: ISSN 0969-2126
PubMed: 36115344
DOI: 10.1016/J.STR.2022.08.008