Fluorine in PDB 8gub: Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719

All present enzymatic activity of Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719:
2.7.1.137; 2.7.1.153; 2.7.11.1;

The binding sites of Fluorine atom in the Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719 (pdb code 8gub). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719, PDB code: 8gub:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1101 b:92.2 occ:1.00 F2 A:1LT1101 0.0 92.2 1.0 C18 A:1LT1101 1.4 92.2 1.0 F A:1LT1101 2.2 92.2 1.0 F1 A:1LT1101 2.2 92.2 1.0 C15 A:1LT1101 2.4 92.2 1.0 H8 A:1LT1101 2.6 92.2 1.0 H5 A:1LT1101 2.7 92.2 1.0 C17 A:1LT1101 2.8 92.2 1.0 H7 A:1LT1101 2.9 92.2 1.0 C16 A:1LT1101 3.0 92.2 1.0 NZ A:LYS802 3.2 90.1 1.0 H6 A:1LT1101 3.4 92.2 1.0 CG A:PRO778 3.4 97.8 1.0 CE A:LYS802 3.5 90.1 1.0 OG A:SER774 3.6 110.4 1.0 CB A:SER774 3.6 110.4 1.0 C13 A:1LT1101 3.7 92.2 1.0 H9 A:1LT1101 3.8 92.2 1.0 H4 A:1LT1101 3.9 92.2 1.0 CD A:PRO778 4.0 97.8 1.0 H3 A:1LT1101 4.3 92.2 1.0 CB A:PRO778 4.4 97.8 1.0 C14 A:1LT1101 4.5 92.2 1.0 N4 A:1LT1101 4.5 92.2 1.0 CD A:LYS802 4.9 90.1 1.0

Fluorine binding site 2 out of 3 in the Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1101 b:92.2 occ:1.00 F A:1LT1101 0.0 92.2 1.0 C18 A:1LT1101 1.4 92.2 1.0 F2 A:1LT1101 2.2 92.2 1.0 F1 A:1LT1101 2.2 92.2 1.0 C15 A:1LT1101 2.4 92.2 1.0 NZ A:LYS802 2.4 90.1 1.0 H6 A:1LT1101 2.5 92.2 1.0 C16 A:1LT1101 2.8 92.2 1.0 C13 A:1LT1101 2.9 92.2 1.0 H5 A:1LT1101 3.1 92.2 1.0 N4 A:1LT1101 3.1 92.2 1.0 CE A:LYS802 3.1 90.1 1.0 CD1 A:ILE848 3.5 82.5 1.0 C17 A:1LT1101 3.7 92.2 1.0 H4 A:1LT1101 3.8 92.2 1.0 H7 A:1LT1101 3.9 92.2 1.0 C14 A:1LT1101 4.0 92.2 1.0 H8 A:1LT1101 4.0 92.2 1.0 C12 A:1LT1101 4.3 92.2 1.0 H3 A:1LT1101 4.4 92.2 1.0 H9 A:1LT1101 4.5 92.2 1.0 CD A:LYS802 4.5 90.1 1.0 CG A:PRO778 4.6 97.8 1.0 CG2 A:ILE800 4.6 83.4 1.0 H2 A:1LT1101 4.8 92.2 1.0 CG A:LYS802 4.9 90.1 1.0 CG1 A:ILE848 4.9 82.5 1.0 C10 A:1LT1101 4.9 92.2 1.0 CB A:PRO778 5.0 97.8 1.0

Fluorine binding site 3 out of 3 in the Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Cryo-Em Structure of Cancer-Specific PI3KALPHA Mutant H1047R in Complex with Byl-719 within 5.0Å range: probe atom residue distance (Å) B Occ A:F1101 b:92.2 occ:1.00 F1 A:1LT1101 0.0 92.2 1.0 C18 A:1LT1101 1.4 92.2 1.0 F2 A:1LT1101 2.2 92.2 1.0 F A:1LT1101 2.2 92.2 1.0 C15 A:1LT1101 2.4 92.2 1.0 H7 A:1LT1101 2.5 92.2 1.0 C13 A:1LT1101 2.8 92.2 1.0 H3 A:1LT1101 2.9 92.2 1.0 C17 A:1LT1101 2.9 92.2 1.0 C14 A:1LT1101 3.0 92.2 1.0 H8 A:1LT1101 3.5 92.2 1.0 CG2 A:ILE800 3.5 83.4 1.0 N4 A:1LT1101 3.7 92.2 1.0 C16 A:1LT1101 3.7 92.2 1.0 H9 A:1LT1101 3.8 92.2 1.0 CG A:PRO778 3.9 97.8 1.0 SD A:MET772 3.9 104.0 1.0 H6 A:1LT1101 4.0 92.2 1.0 H5 A:1LT1101 4.1 92.2 1.0 C10 A:1LT1101 4.1 92.2 1.0 CG1 A:ILE800 4.2 83.4 1.0 NZ A:LYS802 4.2 90.1 1.0 CB A:ILE800 4.2 83.4 1.0 CE A:LYS802 4.3 90.1 1.0 CE A:MET772 4.4 104.0 1.0 H4 A:1LT1101 4.5 92.2 1.0 CB A:PRO778 4.5 97.8 1.0 C12 A:1LT1101 4.6 92.2 1.0 CD1 A:ILE848 4.6 82.5 1.0 CD1 A:ILE800 4.7 83.4 1.0 OG A:SER774 4.7 110.4 1.0 C11 A:1LT1101 4.7 92.2 1.0 C9 A:1LT1101 5.0 92.2 1.0 S A:1LT1101 5.0 92.2 1.0

X.Liu, Q.Zhou, J.R.Hart, Y.Xu, S.Yang, D.Yang, P.K.Vogt, M.W.Wang. Cryo-Em Structures of Cancer-Specific Helical and Kinase Domain Mutations of PI3K Alpha. Proc.Natl.Acad.Sci.Usa V. 119 21119 2022.
ISSN: ESSN 1091-6490
PubMed: 36343266
DOI: 10.1073/PNAS.2215621119