Chlorine in PDB 5swo: Crystal Structure of PI3KALPHA in Complex with Fragments 4 and 19

All present enzymatic activity of Crystal Structure of PI3KALPHA in Complex with Fragments 4 and 19:
2.7.1.153; 2.7.11.1;

The structure of Crystal Structure of PI3KALPHA in Complex with Fragments 4 and 19, PDB code: 5swo was solved by S.B.Gabelli, B.Vogelstein, M.S.Miller, L.M.Amzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	91.81 / 3.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	114.826, 116.360, 149.442, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 27.4

The binding sites of Chlorine atom in the Crystal Structure of PI3KALPHA in Complex with Fragments 4 and 19 (pdb code 5swo). 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 PI3KALPHA in Complex with Fragments 4 and 19, PDB code: 5swo:

Chlorine binding site 1 out of 1 in the Crystal Structure of PI3KALPHA in Complex with Fragments 4 and 19


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 PI3KALPHA in Complex with Fragments 4 and 19 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1101 b:71.4 occ:1.00 O A:GLU849 3.5 89.4 1.0 N A:VAL851 4.0 70.7 1.0 CG2 A:ILE932 4.2 73.1 1.0 CD1 A:TYR836 4.5 76.8 1.0 CA A:VAL850 4.5 79.0 1.0 CE2 A:PHE930 4.6 78.7 1.0 CG A:TYR836 4.6 76.1 1.0 C A:GLU849 4.6 82.6 1.0 CB A:VAL851 4.7 71.3 1.0 C A:VAL850 4.7 75.4 1.0 CE1 A:TYR836 4.7 83.5 1.0 CZ A:PHE930 4.8 74.9 1.0 CG2 A:VAL851 4.8 67.8 1.0 CG2 A:ILE848 4.9 82.1 1.0 SD A:MET922 5.0 87.8 1.0 CA A:VAL851 5.0 75.2 1.0 CD2 A:TYR836 5.0 80.8 1.0

M.S.Miller, S.Maheshwari, F.M.Mcrobb, K.W.Kinzler, L.M.Amzel, B.Vogelstein, S.B.Gabelli. Identification of Allosteric Binding Sites For PI3K Alpha Oncogenic Mutant Specific Inhibitor Design. Bioorg. Med. Chem. V. 25 1481 2017.
ISSN: ESSN 1464-3391
PubMed: 28129991
DOI: 10.1016/J.BMC.2017.01.012