Fluorine in PDB 8tgd: Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA

Enzymatic activity of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA

Protein crystallography data

Fluorine Binding Sites:

Fluorine binding site 1 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 1 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ A:F1511 b:66.5 occ:1.00 F30 A:X3N1511 0.0 66.5 1.0 C29 A:X3N1511 1.3 65.9 1.0 F31 A:X3N1511 2.2 65.8 1.0 C23 A:X3N1511 2.4 65.3 1.0 HE2 A:MET772 2.9 80.3 0.0 HG A:SER774 2.9 83.8 0.0 HE1 A:MET772 3.0 79.7 0.0 HD13 A:ILE800 3.0 65.3 0.0 HG21 A:ILE800 3.1 63.7 0.0 HG3 A:PRO778 3.3 77.3 0.0 N22 A:X3N1511 3.3 64.4 1.0 HG2 A:PRO778 3.3 77.8 0.0 CE A:MET772 3.4 78.7 1.0 N19 A:X3N1511 3.4 62.1 1.0 C25 A:X3N1511 3.6 65.7 1.0 HB2 A:SER774 3.7 83.2 0.0 HB3 A:SER774 3.7 82.6 0.0 C20 A:X3N1511 3.7 62.8 1.0 OG A:SER774 3.8 82.5 1.0 CG A:PRO778 3.8 76.9 1.0 SD A:MET772 3.9 79.8 1.0 CB A:SER774 3.9 81.2 1.0 CD1 A:ILE800 4.1 65.3 1.0 CG2 A:ILE800 4.2 64.0 1.0 HE3 A:MET772 4.4 80.5 0.0 C27 A:X3N1511 4.4 65.6 1.0 HG23 A:ILE800 4.4 63.9 0.0 O26 A:X3N1511 4.5 66.0 1.0 HB2 A:PRO778 4.5 76.1 0.0 HD11 A:ILE800 4.6 65.5 0.0 HB3 A:MET772 4.6 79.7 0.0 HB2 A:MET772 4.6 79.2 0.0 C18 A:X3N1511 4.6 61.7 1.0 HD12 A:ILE800 4.6 64.8 0.0 HZ3 A:LYS802 4.7 80.7 0.0 HG12 A:ILE800 4.7 64.4 0.0 CB A:PRO778 4.7 76.1 1.0 HD3 A:LYS802 4.7 73.7 0.0 HG22 A:ILE800 4.7 63.3 0.0 C10 A:X3N1511 4.8 61.0 1.0 CG1 A:ILE800 4.9 64.2 1.0 HD2 A:PRO778 4.9 77.5 0.0 CD A:PRO778 4.9 76.0 1.0 C21 A:X3N1511 5.0 62.2 1.0

Fluorine binding site 2 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 2 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ A:F1511 b:65.8 occ:1.00 F31 A:X3N1511 0.0 65.8 1.0 C29 A:X3N1511 1.3 65.9 1.0 F30 A:X3N1511 2.2 66.5 1.0 C23 A:X3N1511 2.4 65.3 1.0 N22 A:X3N1511 2.7 64.4 1.0 HG21 A:ILE800 2.9 63.7 0.0 C25 A:X3N1511 3.1 65.7 1.0 HD13 A:ILE848 3.1 57.2 0.0 C27 A:X3N1511 3.1 65.6 1.0 HZ3 A:LYS802 3.2 80.7 0.0 HG3 A:PRO778 3.2 77.3 0.0 HD12 A:ILE848 3.3 57.1 0.0 O26 A:X3N1511 3.3 66.0 1.0 HE2 A:LYS802 3.4 77.3 0.0 C20 A:X3N1511 3.4 62.8 1.0 HD13 A:ILE800 3.5 65.3 0.0 HD3 A:LYS802 3.5 73.7 0.0 CD1 A:ILE848 3.7 58.5 1.0 CG2 A:ILE800 3.8 64.0 1.0 HG A:SER774 3.9 83.8 0.0 N19 A:X3N1511 3.9 62.1 1.0 O28 A:X3N1511 4.0 66.1 1.0 HG22 A:ILE800 4.0 63.3 0.0 NZ A:LYS802 4.0 81.2 1.0 CE A:LYS802 4.1 78.4 1.0 CG A:PRO778 4.1 76.9 1.0 HG2 A:PRO778 4.1 77.8 0.0 HG21 A:ILE848 4.2 57.7 0.0 HD11 A:ILE848 4.3 56.9 0.0 CD A:LYS802 4.3 74.1 1.0 HB2 A:LYS802 4.3 65.5 0.0 HB A:ILE848 4.4 56.9 0.0 HB2 A:PRO778 4.4 76.1 0.0 C21 A:X3N1511 4.4 62.2 1.0 CD1 A:ILE800 4.4 65.3 1.0 HZ1 A:LYS802 4.5 80.4 0.0 HD12 A:ILE800 4.5 64.8 0.0 HB A:ILE800 4.5 62.8 0.0 HB3 A:PRO778 4.5 75.9 0.0 HG23 A:ILE800 4.5 63.9 0.0 CB A:PRO778 4.6 76.1 1.0 O A:HOH1604 4.6 60.2 1.0 HE1 A:MET772 4.7 79.7 0.0 HB3 A:SER774 4.7 82.6 0.0 CB A:ILE800 4.7 63.8 1.0 HZ2 A:LYS802 4.7 80.8 0.0 OG A:SER774 4.8 82.5 1.0 CG1 A:ILE848 4.9 57.9 1.0 HD2 A:LYS802 4.9 73.8 0.0 HE2 A:MET772 5.0 80.3 0.0 C18 A:X3N1511 5.0 61.7 1.0 CB A:ILE848 5.0 58.3 1.0

Fluorine binding site 3 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 3 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ A:F1512 b:69.7 occ:1.00 F1 A:ZWE1512 0.0 69.7 1.0 C5 A:ZWE1512 1.3 69.7 1.0 C6 A:ZWE1512 2.3 69.6 1.0 C4 A:ZWE1512 2.4 70.2 1.0 HZ A:PHE937 2.4 80.3 0.0 HD13 A:LEU911 2.7 72.8 0.0 HZ A:PHE1002 2.9 68.0 0.0 O1 A:ZWE1512 2.9 70.8 1.0 HB3 A:LEU911 3.2 72.0 0.0 HD22 A:LEU911 3.2 73.6 0.0 HG23 A:THR813 3.3 56.8 0.0 HE1 A:PHE1002 3.3 67.5 0.0 CZ A:PHE937 3.4 79.8 1.0 HA A:THR813 3.5 55.6 0.0 C7 A:ZWE1512 3.6 69.9 1.0 C9 A:ZWE1512 3.6 70.4 1.0 CZ A:PHE1002 3.7 67.4 1.0 OG1 A:THR813 3.7 57.9 1.0 CD1 A:LEU911 3.8 72.1 1.0 CE1 A:PHE1002 3.9 67.7 1.0 HE2 A:PHE937 4.0 81.6 0.0 HG13 A:ILE816 4.0 57.7 0.0 CD2 A:LEU911 4.1 72.3 1.0 CB A:LEU911 4.1 70.5 1.0 C8 A:ZWE1512 4.1 70.0 1.0 CE2 A:PHE937 4.2 80.2 1.0 CG2 A:THR813 4.2 56.9 1.0 C3 A:ZWE1512 4.2 71.5 1.0 CG A:LEU911 4.2 71.7 1.0 HE1 A:PHE937 4.3 80.2 0.0 CB A:THR813 4.3 56.8 1.0 HD11 A:LEU911 4.3 73.0 0.0 CE1 A:PHE937 4.3 80.2 1.0 HD11 A:ILE913 4.3 74.5 0.0 CA A:THR813 4.3 56.4 1.0 HD12 A:LEU911 4.4 73.2 0.0 HG1 A:THR813 4.5 56.9 0.0 F5 A:ZWE1512 4.5 73.7 1.0 HG21 A:THR813 4.5 56.7 0.0 C2 A:ZWE1512 4.6 71.1 1.0 HG A:LEU812 4.6 58.2 0.0 F2 A:ZWE1512 4.6 70.3 1.0 HD21 A:LEU911 4.7 73.7 0.0 HB2 A:LEU911 4.7 72.4 0.0 HB A:ILE816 4.7 56.8 0.0 HG21 A:ILE816 4.7 58.2 0.0 CE2 A:PHE1002 4.9 67.7 1.0 HD23 A:LEU911 4.9 74.4 0.0 N A:THR813 4.9 56.6 1.0 CG1 A:ILE816 4.9 57.9 1.0

Fluorine binding site 4 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 4 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ A:F1512 b:70.3 occ:1.00 F2 A:ZWE1512 0.0 70.3 1.0 C7 A:ZWE1512 1.3 69.9 1.0 HD23 A:LEU812 2.2 58.5 0.0 C6 A:ZWE1512 2.3 69.6 1.0 C8 A:ZWE1512 2.3 70.0 1.0 HG3 A:GLN809 2.4 71.5 0.0 HA A:GLN809 2.7 65.0 0.0 HE1 A:MET1010 2.8 82.2 0.0 HB3 A:LEU812 2.9 56.4 0.0 HE2 A:MET1010 3.2 82.5 0.0 CD2 A:LEU812 3.2 59.6 1.0 CE A:MET1010 3.4 83.7 1.0 CG A:GLN809 3.5 72.3 1.0 C5 A:ZWE1512 3.6 69.7 1.0 C9 A:ZWE1512 3.6 70.4 1.0 HD12 A:LEU1013 3.6 90.0 0.0 CA A:GLN809 3.6 66.6 1.0 HD11 A:LEU1013 3.7 90.4 0.0 HG A:LEU812 3.7 58.2 0.0 HD22 A:LEU812 3.8 58.2 0.0 HE3 A:MET1010 3.8 82.0 0.0 O A:GLN809 3.8 65.7 1.0 CG A:LEU812 3.8 59.3 1.0 HD21 A:LEU812 3.8 58.8 0.0 CB A:LEU812 3.8 58.0 1.0 HE1 A:PHE1002 3.9 67.5 0.0 CB A:GLN809 3.9 68.8 1.0 HG2 A:GLN809 3.9 71.4 0.0 C4 A:ZWE1512 4.0 70.2 1.0 HB2 A:GLN809 4.0 67.5 0.0 HG1 A:THR813 4.1 56.9 0.0 CD1 A:LEU1013 4.1 90.6 1.0 C A:GLN809 4.2 65.8 1.0 HB2 A:LEU812 4.3 56.1 0.0 OG1 A:THR813 4.4 57.9 1.0 HD11 A:LEU938 4.4 86.8 0.0 HB2 A:GLU1012 4.4 92.8 0.0 CD A:GLN809 4.5 77.0 1.0 HG A:LEU1013 4.5 90.3 0.0 H A:THR813 4.5 55.1 0.0 F1 A:ZWE1512 4.6 69.7 1.0 HD12 A:LEU938 4.7 86.5 0.0 N A:GLN809 4.7 66.5 1.0 HZ A:PHE937 4.7 80.3 0.0 HE21 A:GLN809 4.8 77.3 0.0 O A:ARG808 4.8 66.8 1.0 H A:LEU812 4.9 57.0 0.0 N A:THR813 4.9 56.6 1.0 CE1 A:PHE1002 4.9 67.7 1.0 CG A:LEU1013 4.9 90.1 1.0 C2 A:ZWE1512 4.9 71.1 1.0 HD1 A:PHE1002 5.0 67.1 0.0 HD13 A:LEU1013 5.0 90.3 0.0 HB3 A:GLN809 5.0 67.4 0.0 CA A:LEU812 5.0 58.2 1.0 SD A:MET1010 5.0 84.3 1.0

Fluorine binding site 5 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 5 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ A:F1512 b:73.6 occ:1.00 F3 A:ZWE1512 0.0 73.6 1.0 C16 A:ZWE1512 1.3 73.5 1.0 F4 A:ZWE1512 2.1 73.8 1.0 F5 A:ZWE1512 2.2 73.7 1.0 C10 A:ZWE1512 2.4 72.9 1.0 C3 A:ZWE1512 2.8 71.5 1.0 HB A:ILE1022 2.9 93.5 0.0 HA A:ILE1019 3.1 95.6 0.0 O1 A:ZWE1512 3.2 70.8 1.0 HG23 A:ILE1019 3.3 95.8 0.0 CE2 A:PHE1002 3.4 67.7 1.0 HD12 A:ILE1022 3.5 94.5 0.0 HE2 A:PHE1002 3.5 69.2 0.0 N1 A:ZWE1512 3.6 73.9 1.0 C2 A:ZWE1512 3.7 71.1 1.0 CD2 A:PHE1002 3.7 67.1 1.0 CZ A:PHE1002 3.8 67.4 1.0 H A:ILE1022 3.9 94.5 0.0 HD2 A:PHE1002 4.0 68.8 0.0 CB A:ILE1022 4.0 90.0 1.0 O A:ILE1019 4.1 93.2 1.0 HZ A:PHE1002 4.1 68.0 0.0 CA A:ILE1019 4.1 92.8 1.0 C4 A:ZWE1512 4.1 70.2 1.0 HG22 A:ILE1019 4.2 96.8 0.0 CG2 A:ILE1019 4.2 93.3 1.0 HG21 A:ILE1022 4.3 93.9 0.0 O A:ASP1018 4.3 94.4 1.0 CG A:PHE1002 4.3 66.6 1.0 CE1 A:PHE1002 4.4 67.7 1.0 CD1 A:ILE1022 4.4 91.9 1.0 C1 A:ZWE1512 4.4 71.2 1.0 C9 A:ZWE1512 4.4 70.4 1.0 HD22 A:LEU911 4.5 73.6 0.0 CD1 A:PHE1002 4.6 67.1 1.0 HA A:LEU911 4.6 73.1 0.0 HG12 A:ILE1019 4.6 95.4 0.0 C A:ILE1019 4.6 92.9 1.0 HD21 A:LEU1013 4.6 91.4 0.0 CG2 A:ILE1022 4.6 90.2 1.0 N A:ILE1022 4.6 90.2 1.0 CG1 A:ILE1022 4.6 90.8 1.0 HB3 A:TYR1021 4.7 95.2 0.0 CB A:ILE1019 4.7 92.9 1.0 HD23 A:LEU911 4.8 74.4 0.0 HD13 A:ILE1022 4.8 95.0 0.0 C11 A:ZWE1512 4.8 75.0 1.0 HG13 A:ILE1022 4.8 94.6 0.0 HG22 A:ILE1022 4.8 94.5 0.0 CA A:ILE1022 4.8 90.0 1.0 HD2 A:TYR1021 4.9 97.3 0.0 HE1 A:PHE1002 5.0 67.5 0.0

Fluorine binding site 6 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 6 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ A:F1512 b:73.8 occ:1.00 F4 A:ZWE1512 0.0 73.8 1.0 C16 A:ZWE1512 1.3 73.5 1.0 F3 A:ZWE1512 2.1 73.6 1.0 F5 A:ZWE1512 2.1 73.7 1.0 HB A:ILE1022 2.3 93.5 0.0 C10 A:ZWE1512 2.4 72.9 1.0 H A:ILE1022 2.6 94.5 0.0 HD2 A:TYR1021 2.8 97.3 0.0 N1 A:ZWE1512 2.9 73.9 1.0 HB3 A:TYR1021 2.9 95.2 0.0 N A:ILE1022 3.0 90.2 1.0 CB A:ILE1022 3.2 90.0 1.0 CA A:ILE1022 3.4 90.0 1.0 HA A:ILE1022 3.4 94.6 0.0 C3 A:ZWE1512 3.7 71.5 1.0 O A:ILE1019 3.7 93.2 1.0 C A:TYR1021 3.8 90.8 1.0 HA A:ILE1019 3.8 95.6 0.0 C11 A:ZWE1512 3.8 75.0 1.0 CD2 A:TYR1021 3.8 93.2 1.0 HD12 A:ILE1022 3.9 94.5 0.0 HA A:LEU911 3.9 73.1 0.0 CB A:TYR1021 3.9 91.0 1.0 HG13 A:ILE1022 3.9 94.6 0.0 CG1 A:ILE1022 4.1 90.8 1.0 O1 A:ZWE1512 4.1 70.8 1.0 O2 A:ZWE1512 4.1 75.3 1.0 CA A:TYR1021 4.2 91.0 1.0 CG2 A:ILE1022 4.3 90.2 1.0 H A:TYR1021 4.3 95.8 0.0 CG A:TYR1021 4.4 91.9 1.0 HG22 A:ILE1022 4.4 94.5 0.0 O A:ILE910 4.4 69.2 1.0 C A:ILE1019 4.4 92.9 1.0 O A:ASP1018 4.5 94.4 1.0 N A:TYR1021 4.5 91.1 1.0 HG21 A:ILE1022 4.5 93.9 0.0 CD1 A:ILE1022 4.5 91.9 1.0 CA A:ILE1019 4.6 92.8 1.0 O A:TYR1021 4.6 91.2 1.0 O A:LEU911 4.7 72.1 1.0 HG23 A:ILE1019 4.7 95.8 0.0 HZ1 A:LYS941 4.7 121.1 0.0 HB2 A:TYR1021 4.7 96.0 0.0 N2 A:ZWE1512 4.8 75.7 1.0 HG22 A:ILE1019 4.8 96.8 0.0 HD23 A:LEU911 4.8 74.4 0.0 C2 A:ZWE1512 4.8 71.1 1.0 CA A:LEU911 4.9 70.5 1.0 HE2 A:PHE1002 4.9 69.2 0.0 CE2 A:TYR1021 4.9 94.3 1.0 C A:ILE1022 4.9 90.2 1.0 C A:LEU911 5.0 71.5 1.0

Fluorine binding site 7 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 7 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ A:F1512 b:73.7 occ:1.00 F5 A:ZWE1512 0.0 73.7 1.0 C16 A:ZWE1512 1.4 73.5 1.0 F4 A:ZWE1512 2.1 73.8 1.0 F3 A:ZWE1512 2.2 73.6 1.0 HA A:LEU911 2.4 73.1 0.0 C10 A:ZWE1512 2.5 72.9 1.0 O1 A:ZWE1512 2.7 70.8 1.0 N1 A:ZWE1512 2.7 73.9 1.0 C3 A:ZWE1512 3.0 71.5 1.0 HD22 A:LEU911 3.1 73.6 0.0 HD23 A:LEU911 3.2 74.4 0.0 HD12 A:ILE1022 3.3 94.5 0.0 HB A:ILE1022 3.3 93.5 0.0 CA A:LEU911 3.4 70.5 1.0 HB3 A:LEU911 3.5 72.0 0.0 O A:LEU911 3.6 72.1 1.0 CD2 A:LEU911 3.6 72.3 1.0 HE2 A:PHE1002 3.8 69.2 0.0 C A:LEU911 3.9 71.5 1.0 HD2 A:TYR1021 3.9 97.3 0.0 HZ A:PHE1002 3.9 68.0 0.0 CB A:LEU911 3.9 70.5 1.0 C4 A:ZWE1512 3.9 70.2 1.0 HG13 A:ILE1022 4.1 94.6 0.0 C11 A:ZWE1512 4.1 75.0 1.0 CE2 A:PHE1002 4.1 67.7 1.0 O A:ILE910 4.1 69.2 1.0 CZ A:PHE1002 4.2 67.4 1.0 CD1 A:ILE1022 4.2 91.9 1.0 CB A:ILE1022 4.3 90.0 1.0 C2 A:ZWE1512 4.3 71.1 1.0 CG1 A:ILE1022 4.4 90.8 1.0 CG A:LEU911 4.4 71.7 1.0 N A:LEU911 4.5 69.9 1.0 F1 A:ZWE1512 4.5 69.7 1.0 HD21 A:LEU911 4.5 73.7 0.0 HA A:ILE1022 4.6 94.6 0.0 H A:ILE1022 4.6 94.5 0.0 HE2 A:PHE937 4.6 81.6 0.0 C5 A:ZWE1512 4.7 69.7 1.0 HD11 A:ILE1022 4.7 94.9 0.0 C A:ILE910 4.7 69.5 1.0 C9 A:ZWE1512 4.8 70.4 1.0 HB3 A:TYR1021 4.8 95.2 0.0 N2 A:ZWE1512 4.8 75.7 1.0 O2 A:ZWE1512 4.8 75.3 1.0 CA A:ILE1022 4.8 90.0 1.0 N A:ILE1022 4.9 90.2 1.0 HB2 A:LEU911 4.9 72.4 0.0 CD2 A:TYR1021 5.0 93.2 1.0 CD2 A:PHE1002 5.0 67.1 1.0

Fluorine binding site 8 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 8 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ C:F1504 b:111.1 occ:1.00 F30 C:X3N1504 0.0 111.1 1.0 C29 C:X3N1504 1.3 111.0 1.0 F31 C:X3N1504 2.1 111.2 1.0 C23 C:X3N1504 2.4 110.8 1.0 HG C:SER774 2.9 121.2 0.0 HD13 C:ILE800 3.0 99.6 0.0 HE1 C:MET772 3.1 118.1 0.0 HG21 C:ILE800 3.1 97.2 0.0 HG3 C:PRO778 3.3 113.5 0.0 N22 C:X3N1504 3.3 110.6 1.0 HG2 C:PRO778 3.3 113.8 0.0 HE2 C:MET772 3.3 119.5 0.0 N19 C:X3N1504 3.4 110.1 1.0 CE C:MET772 3.5 115.4 1.0 C25 C:X3N1504 3.6 110.8 1.0 HB2 C:SER774 3.7 120.5 0.0 SD C:MET772 3.7 116.5 1.0 HB3 C:SER774 3.7 119.5 0.0 C20 C:X3N1504 3.7 110.3 1.0 CG C:PRO778 3.8 111.3 1.0 OG C:SER774 3.8 116.5 1.0 CB C:SER774 4.0 114.8 1.0 CD1 C:ILE800 4.1 99.1 1.0 CG2 C:ILE800 4.2 97.3 1.0 C27 C:X3N1504 4.4 111.0 1.0 HG23 C:ILE800 4.4 97.2 0.0 HB3 C:MET772 4.5 116.0 0.0 O26 C:X3N1504 4.5 111.0 1.0 HB2 C:PRO778 4.5 111.2 0.0 HD11 C:ILE800 4.6 99.7 0.0 HE3 C:MET772 4.6 119.0 0.0 C18 C:X3N1504 4.6 109.8 1.0 HD12 C:ILE800 4.6 98.5 0.0 HB2 C:MET772 4.6 114.9 0.0 HZ3 C:LYS802 4.7 118.3 0.0 HG12 C:ILE800 4.7 97.9 0.0 CB C:PRO778 4.7 110.6 1.0 HD3 C:LYS802 4.7 110.7 0.0 HG22 C:ILE800 4.7 96.3 0.0 C10 C:X3N1504 4.8 109.6 1.0 CG1 C:ILE800 4.9 97.8 1.0 HD2 C:PRO778 4.9 114.2 0.0 CD C:PRO778 4.9 110.1 1.0 CB C:MET772 4.9 111.0 1.0 C21 C:X3N1504 5.0 110.0 1.0

Fluorine binding site 9 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 9 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ C:F1504 b:111.2 occ:1.00 F31 C:X3N1504 0.0 111.2 1.0 C29 C:X3N1504 1.3 111.0 1.0 F30 C:X3N1504 2.1 111.1 1.0 C23 C:X3N1504 2.4 110.8 1.0 N22 C:X3N1504 2.6 110.6 1.0 HG21 C:ILE800 2.8 97.2 0.0 C25 C:X3N1504 3.1 110.8 1.0 C27 C:X3N1504 3.1 111.0 1.0 HD13 C:ILE848 3.1 101.4 0.0 HZ3 C:LYS802 3.2 118.3 0.0 HG3 C:PRO778 3.2 113.5 0.0 HD12 C:ILE848 3.3 100.9 0.0 O26 C:X3N1504 3.3 111.0 1.0 HE2 C:LYS802 3.4 113.9 0.0 C20 C:X3N1504 3.4 110.3 1.0 HD13 C:ILE800 3.5 99.6 0.0 HD3 C:LYS802 3.5 110.7 0.0 CD1 C:ILE848 3.7 102.5 1.0 CG2 C:ILE800 3.8 97.3 1.0 HG C:SER774 3.9 121.2 0.0 N19 C:X3N1504 3.9 110.1 1.0 O28 C:X3N1504 4.0 111.2 1.0 HG22 C:ILE800 4.0 96.3 0.0 NZ C:LYS802 4.0 116.9 1.0 HG2 C:PRO778 4.1 113.8 0.0 CG C:PRO778 4.1 111.3 1.0 CE C:LYS802 4.1 114.2 1.0 HG21 C:ILE848 4.2 99.3 0.0 HD11 C:ILE848 4.3 100.9 0.0 CD C:LYS802 4.3 109.8 1.0 HB2 C:LYS802 4.3 99.4 0.0 HB C:ILE848 4.4 98.0 0.0 HB2 C:PRO778 4.4 111.2 0.0 C21 C:X3N1504 4.4 110.0 1.0 CD1 C:ILE800 4.4 99.1 1.0 HZ1 C:LYS802 4.5 118.0 0.0 HD12 C:ILE800 4.5 98.5 0.0 HB C:ILE800 4.5 95.2 0.0 HB3 C:PRO778 4.5 111.3 0.0 HG23 C:ILE800 4.5 97.2 0.0 CB C:PRO778 4.6 110.6 1.0 HB3 C:SER774 4.7 119.5 0.0 CB C:ILE800 4.7 96.8 1.0 HZ2 C:LYS802 4.7 119.0 0.0 HE1 C:MET772 4.8 118.1 0.0 OG C:SER774 4.8 116.5 1.0 CG1 C:ILE848 4.9 101.3 1.0 HD2 C:LYS802 4.9 111.4 0.0 C18 C:X3N1504 5.0 109.8 1.0

Fluorine binding site 10 out of 14 in 8tgd

Fluorine Binding Sites List in 8tgd

Fluorine binding site 10 out of 14 in the Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of Stx-478, A Mutant-Selective, Allosteric Inhibitor Bound to H1047R PI3KALPHA within 5.0Å range: probe atom residue distance (Å) B Occ C:F1505 b:108.7 occ:1.00 F1 C:ZWE1505 0.0 108.7 1.0 C5 C:ZWE1505 1.3 108.8 1.0 C6 C:ZWE1505 2.3 108.7 1.0 C4 C:ZWE1505 2.3 109.3 1.0 HZ C:PHE937 2.4 133.4 0.0 HD13 C:LEU911 2.7 122.7 0.0 O1 C:ZWE1505 2.9 109.7 1.0 HZ C:PHE1002 2.9 108.9 0.0 HB3 C:LEU911 3.2 122.9 0.0 HD22 C:LEU911 3.2 123.3 0.0 HG23 C:THR813 3.3 88.9 0.0 HE1 C:PHE1002 3.4 108.5 0.0 CZ C:PHE937 3.4 131.0 1.0 HA C:THR813 3.5 86.3 0.0 C7 C:ZWE1505 3.6 108.7 1.0 C9 C:ZWE1505 3.6 109.3 1.0 CZ C:PHE1002 3.7 108.3 1.0 OG1 C:THR813 3.7 88.8 1.0 CD1 C:LEU911 3.8 121.5 1.0 CE1 C:PHE1002 3.9 108.6 1.0 HE2 C:PHE937 4.0 135.8 0.0 HG13 C:ILE816 4.0 90.7 0.0 CD2 C:LEU911 4.1 121.5 1.0 CB C:LEU911 4.1 119.6 1.0 C8 C:ZWE1505 4.1 109.0 1.0 CE2 C:PHE937 4.2 131.2 1.0 CG2 C:THR813 4.2 88.5 1.0 C3 C:ZWE1505 4.2 110.1 1.0 CG C:LEU911 4.2 120.9 1.0 CB C:THR813 4.3 88.2 1.0 HD11 C:LEU911 4.3 122.2 0.0 HE1 C:PHE937 4.3 133.2 0.0 CA C:THR813 4.3 87.5 1.0 HD11 C:ILE913 4.4 125.2 0.0 CE1 C:PHE937 4.4 131.1 1.0 HD12 C:LEU911 4.4 123.3 0.0 HG1 C:THR813 4.5 88.2 0.0 F5 C:ZWE1505 4.5 111.2 1.0 HG21 C:THR813 4.5 89.3 0.0 C2 C:ZWE1505 4.6 109.6 1.0 HG C:LEU812 4.6 88.5 0.0 F2 C:ZWE1505 4.6 108.7 1.0 HD21 C:LEU911 4.7 122.8 0.0 HB2 C:LEU911 4.7 123.5 0.0 HB C:ILE816 4.7 89.1 0.0 HG21 C:ILE816 4.7 90.6 0.0 CE2 C:PHE1002 4.9 108.5 1.0 HD23 C:LEU911 4.9 124.2 0.0 N C:THR813 4.9 87.8 1.0 HD11 C:LEU938 4.9 136.3 0.0 CG1 C:ILE816 4.9 91.9 1.0

Reference: