Bromine in PDB 5sxe: Crystal Structure of PI3KALPHA in Complex with Fragments 19 and 28

All present enzymatic activity of Crystal Structure of PI3KALPHA in Complex with Fragments 19 and 28:
2.7.1.153; 2.7.11.1;

The structure of Crystal Structure of PI3KALPHA in Complex with Fragments 19 and 28, PDB code: 5sxe 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)	91.65 / 3.51
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	113.827, 116.261, 148.977, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 27.1

The binding sites of Bromine atom in the Crystal Structure of PI3KALPHA in Complex with Fragments 19 and 28 (pdb code 5sxe). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of PI3KALPHA in Complex with Fragments 19 and 28, PDB code: 5sxe:

Bromine binding site 1 out of 1 in the Crystal Structure of PI3KALPHA in Complex with Fragments 19 and 28


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 PI3KALPHA in Complex with Fragments 19 and 28 within 5.0Å range: probe atom residue distance (Å) B Occ B:Br701 b:0.0 occ:1.00 BR01 B:ES3701 0.0 0.0 1.0 C02 B:ES3701 2.0 0.7 1.0 N06 B:ES3701 3.0 0.6 1.0 C03 B:ES3701 3.0 0.2 1.0 OE2 B:GLU489 3.5 0.0 1.0 OE1 A:GLU78 3.6 0.0 1.0 CD B:GLU489 3.9 0.1 1.0 C05 B:ES3701 4.1 0.7 1.0 N04 B:ES3701 4.1 0.3 1.0 CD A:ARG79 4.2 0.1 1.0 OE1 B:GLU489 4.4 0.8 1.0 O A:ALA77 4.6 0.2 1.0 CG B:GLU489 4.6 0.0 1.0 CD A:GLU78 4.6 0.7 1.0 CG A:ARG79 4.7 0.6 1.0 N A:ARG79 4.9 0.3 1.0 CA A:GLU78 4.9 0.3 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