Fluorine in PDB 8e1o: Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder

The structure of Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder, PDB code: 8e1o was solved by C.L.Noland, A.Dey, J.Zbieg, J.Crawford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.89 / 2.25
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	122.15, 62.069, 79.856, 90, 117.41, 90
R / Rfree (%)	20 / 24.7

The binding sites of Fluorine atom in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder (pdb code 8e1o). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder, PDB code: 8e1o:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:45.8 occ:1.00 F33 A:Y2S602 0.0 45.8 1.0 C32 A:Y2S602 1.4 42.1 1.0 F34 A:Y2S602 2.3 43.4 1.0 F35 A:Y2S602 2.3 35.9 1.0 C28 A:Y2S602 2.4 34.8 1.0 C30 A:Y2S602 2.7 39.2 1.0 CB A:ALA304 3.0 41.3 1.0 C27 A:Y2S602 3.1 32.2 1.0 CD2 A:LEU306 3.3 42.0 1.0 CD2 A:LEU387 3.5 36.7 1.0 CG A:LEU306 4.1 40.3 1.0 C31 A:Y2S602 4.2 38.0 1.0 CD1 A:LEU306 4.4 39.8 1.0 C26 A:Y2S602 4.5 33.2 1.0 CA A:ALA304 4.5 33.8 1.0 CB A:PHE251 4.6 27.5 1.0 C24 A:Y2S602 4.7 30.9 1.0 CG A:LEU387 4.8 30.6 1.0 CD2 A:LEU390 4.9 36.0 1.0 CD2 A:PHE428 4.9 27.9 1.0

Fluorine binding site 2 out of 6 in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:43.4 occ:1.00 F34 A:Y2S602 0.0 43.4 1.0 C32 A:Y2S602 1.4 42.1 1.0 F33 A:Y2S602 2.3 45.8 1.0 F35 A:Y2S602 2.3 35.9 1.0 C28 A:Y2S602 2.4 34.8 1.0 C27 A:Y2S602 2.7 32.2 1.0 CD2 A:LEU387 3.4 36.7 1.0 CD2 A:LEU390 3.5 36.0 1.0 C30 A:Y2S602 3.7 39.2 1.0 CE2 A:PHE386 3.9 28.3 1.0 CD2 A:LEU403 4.0 33.9 1.0 CD2 A:PHE386 4.1 25.8 1.0 C26 A:Y2S602 4.1 33.2 1.0 CG A:LEU387 4.3 30.6 1.0 CD2 A:LEU306 4.4 42.0 1.0 CD1 A:LEU306 4.7 39.8 1.0 CD1 A:LEU403 4.7 34.7 1.0 CG A:LEU390 4.8 28.5 1.0 C31 A:Y2S602 4.9 38.0 1.0 CE1 A:PHE406 5.0 23.7 1.0 CB A:ALA304 5.0 41.3 1.0 CZ A:PHE386 5.0 28.1 1.0 CB A:LEU390 5.0 29.1 1.0 CG A:LEU403 5.0 28.3 1.0 C24 A:Y2S602 5.0 30.9 1.0

Fluorine binding site 3 out of 6 in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:35.9 occ:1.00 F35 A:Y2S602 0.0 35.9 1.0 C32 A:Y2S602 1.4 42.1 1.0 F33 A:Y2S602 2.3 45.8 1.0 F34 A:Y2S602 2.3 43.4 1.0 C28 A:Y2S602 2.4 34.8 1.0 C30 A:Y2S602 3.1 39.2 1.0 CD2 A:PHE428 3.3 27.9 1.0 CB A:ALA304 3.7 41.3 1.0 CB A:PHE428 3.7 27.1 1.0 CD1 A:LEU403 3.7 34.7 1.0 C27 A:Y2S602 3.7 32.2 1.0 CG A:PHE428 3.7 24.8 1.0 CD2 A:LEU403 3.7 33.9 1.0 CE2 A:PHE428 4.2 26.2 1.0 C31 A:Y2S602 4.4 38.0 1.0 CG A:LEU403 4.4 28.3 1.0 CE1 A:PHE406 4.6 23.7 1.0 CD2 A:LEU390 4.7 36.0 1.0 CD1 A:PHE428 4.7 26.9 1.0 C26 A:Y2S602 4.8 33.2 1.0 O A:GLU429 4.9 29.4 1.0 CD1 A:PHE406 4.9 23.9 1.0 CA A:PHE428 5.0 25.1 1.0

Fluorine binding site 4 out of 6 in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:40.8 occ:1.00 F33 B:Y2S501 0.0 40.8 1.0 C32 B:Y2S501 1.4 35.7 1.0 F35 B:Y2S501 2.2 37.2 1.0 F34 B:Y2S501 2.3 32.9 1.0 C28 B:Y2S501 2.4 29.9 1.0 C30 B:Y2S501 2.8 33.5 1.0 C27 B:Y2S501 3.0 25.3 1.0 CD2 B:LEU306 3.4 52.7 1.0 CD2 B:LEU387 3.4 40.5 1.0 CG B:LEU306 3.7 43.4 1.0 CD1 B:LEU306 3.7 42.4 1.0 CB B:ALA304 3.7 29.9 1.0 C31 B:Y2S501 4.3 25.3 1.0 CG B:LEU387 4.4 40.5 1.0 C26 B:Y2S501 4.4 28.8 1.0 CD2 B:LEU390 4.4 33.3 1.0 C24 B:Y2S501 4.7 27.1 1.0 CB B:PHE251 4.7 33.0 1.0 CD1 B:LEU387 5.0 33.0 1.0

Fluorine binding site 5 out of 6 in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:32.9 occ:1.00 F34 B:Y2S501 0.0 32.9 1.0 C32 B:Y2S501 1.4 35.7 1.0 F35 B:Y2S501 2.3 37.2 1.0 F33 B:Y2S501 2.3 40.8 1.0 C28 B:Y2S501 2.4 29.9 1.0 CB B:ALA304 2.9 29.9 1.0 C30 B:Y2S501 3.1 33.5 1.0 C27 B:Y2S501 3.7 25.3 1.0 CB B:PHE428 4.0 24.1 1.0 O B:GLU429 4.0 26.6 1.0 CD1 B:LEU403 4.0 28.1 1.0 CD2 B:PHE428 4.1 24.8 1.0 CA B:ALA304 4.3 28.1 1.0 CG B:PHE428 4.3 22.7 1.0 C31 B:Y2S501 4.3 25.3 1.0 CD2 B:LEU403 4.6 24.7 1.0 N B:ALA304 4.6 29.4 1.0 C26 B:Y2S501 4.8 28.8 1.0 CG2 B:VAL430 4.8 25.8 1.0 C B:GLU429 4.8 24.6 1.0 CD1 B:LEU306 4.8 42.4 1.0 CG1 B:VAL252 4.9 33.2 1.0 CG B:LEU403 5.0 23.5 1.0

Fluorine binding site 6 out of 6 in the Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of HTEAD2 Bound to A Methoxypyridine Lipid Pocket Binder within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:37.2 occ:1.00 F35 B:Y2S501 0.0 37.2 1.0 C32 B:Y2S501 1.4 35.7 1.0 F33 B:Y2S501 2.2 40.8 1.0 F34 B:Y2S501 2.3 32.9 1.0 C28 B:Y2S501 2.4 29.9 1.0 C27 B:Y2S501 2.8 25.3 1.0 CD2 B:LEU403 3.3 24.7 1.0 CD2 B:LEU390 3.4 33.3 1.0 C30 B:Y2S501 3.7 33.5 1.0 CD1 B:LEU403 3.8 28.1 1.0 C26 B:Y2S501 4.1 28.8 1.0 CG B:LEU403 4.1 23.5 1.0 CE2 B:PHE386 4.4 29.5 1.0 CD2 B:LEU387 4.6 40.5 1.0 CD1 B:LEU306 4.7 42.4 1.0 CB B:PHE428 4.8 24.1 1.0 CE1 B:PHE406 4.8 37.7 1.0 CD2 B:PHE386 4.8 29.1 1.0 C31 B:Y2S501 4.9 25.3 1.0 CG B:LEU390 4.9 29.7 1.0 CB B:ALA304 5.0 29.9 1.0

T.Pham, K.Pahuja, Z.Zbieg, C.L.Noland, H.J.Lee, T.Hagenbeek, C.Rose, K.Browder, V.Pham, M.Yu, M.L.Chu, S.Martin, E.Verschueren, J.Li, M.Kubala, R.Fong, M.Lorenzo, E.Villemure, W.Lee, T.Cheung, S.Clausen, J.Lacap, Y.Liang, J.Cheng, S.Schmidt, Z.Modrusan, M.Cohen, J.Crawford, J.Heinrich, A.Ashworth, J.Lill, S.Malek, I.Wertz, J.Rudolph, A.Dey, M.Chang. Targeting the Hippo Pathway in Cancers Via Ubiquitination Dependent Tead Degradation To Be Published.