Fluorine in PDB 6e5g: Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator

The structure of Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator, PDB code: 6e5g was solved by K.Bum-Erdene, G.Gonzalez-Gutierrez, S.O.Meroueh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.89 / 2.43
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	123.757, 61.226, 79.839, 90.00, 116.89, 90.00
R / Rfree (%)	22.1 / 26.8

The binding sites of Fluorine atom in the Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator (pdb code 6e5g). 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 Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator, PDB code: 6e5g:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator


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 Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:80.3 occ:1.00 F1 B:HUY501 0.0 80.3 1.0 C16 B:HUY501 1.4 80.6 1.0 F3 B:HUY501 2.2 65.2 1.0 F2 B:HUY501 2.2 0.1 1.0 C15 B:HUY501 2.4 80.3 1.0 HD21 B:LEU383 2.5 87.2 1.0 HD11 B:ILE408 2.8 57.5 1.0 HD12 B:ILE408 2.9 57.5 1.0 CD1 B:ILE408 3.1 47.9 1.0 HD13 B:ILE408 3.1 57.5 1.0 C17 B:HUY501 3.2 82.1 1.0 C14 B:HUY501 3.3 82.3 1.0 CD2 B:LEU383 3.4 72.7 1.0 HD23 B:LEU383 3.6 87.2 1.0 HZ B:PHE428 3.8 55.4 1.0 HD11 B:LEU383 3.9 66.9 1.0 HZ B:PHE406 3.9 48.1 1.0 HD22 B:LEU383 4.0 87.2 1.0 HG B:LEU383 4.0 82.5 1.0 CG B:LEU383 4.2 68.8 1.0 CZ B:PHE428 4.2 46.2 1.0 HE2 B:PHE428 4.2 52.3 1.0 HE1 B:PHE406 4.4 49.7 1.0 C11 B:HUY501 4.4 82.7 1.0 CE2 B:PHE428 4.5 43.6 1.0 C13 B:HUY501 4.5 85.0 1.0 HB2 B:ALA235 4.5 45.2 1.0 CD1 B:LEU383 4.5 55.7 1.0 CG1 B:ILE408 4.6 40.0 1.0 CZ B:PHE406 4.7 40.1 1.0 HB1 B:ALA235 4.7 45.2 1.0 HG13 B:ILE408 4.8 47.9 1.0 HE2 B:MET379 4.9 57.1 1.0 HB3 B:ALA235 4.9 45.2 1.0 HG21 B:ILE408 4.9 56.4 1.0 CE1 B:PHE406 4.9 41.4 1.0 CB B:ALA235 4.9 37.6 1.0 HG12 B:ILE408 5.0 47.9 1.0 C12 B:HUY501 5.0 87.2 1.0 HD13 B:LEU383 5.0 66.9 1.0

Fluorine binding site 2 out of 6 in the Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator


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 Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:0.1 occ:1.00 F2 B:HUY501 0.0 0.1 1.0 C16 B:HUY501 1.4 80.6 1.0 F3 B:HUY501 2.2 65.2 1.0 F1 B:HUY501 2.2 80.3 1.0 C15 B:HUY501 2.4 80.3 1.0 HD21 B:LEU383 2.8 87.2 1.0 C17 B:HUY501 2.8 82.1 1.0 HB2 B:ALA235 2.9 45.2 1.0 HE2 B:MET379 2.9 57.1 1.0 HB1 B:ALA235 2.9 45.2 1.0 HD23 B:LEU383 2.9 87.2 1.0 HG22 B:VAL329 3.2 68.5 1.0 CB B:ALA235 3.3 37.6 1.0 CD2 B:LEU383 3.3 72.7 1.0 HG21 B:VAL329 3.4 68.5 1.0 C14 B:HUY501 3.5 82.3 1.0 HB3 B:ALA235 3.7 45.2 1.0 CG2 B:VAL329 3.7 57.1 1.0 CE B:MET379 3.8 47.6 1.0 HD22 B:LEU383 3.8 87.2 1.0 HE1 B:MET379 4.0 57.1 1.0 HG3 B:MET379 4.1 70.4 1.0 HG23 B:VAL329 4.1 68.5 1.0 C11 B:HUY501 4.2 82.7 1.0 SD B:MET379 4.4 46.8 1.0 HG B:LEU383 4.5 82.5 1.0 HE3 B:MET379 4.5 57.1 1.0 CG B:LEU383 4.5 68.8 1.0 HD13 B:ILE408 4.6 57.5 1.0 CA B:ALA235 4.7 42.0 1.0 C13 B:HUY501 4.7 85.0 1.0 HA B:ALA235 4.7 50.4 1.0 HD11 B:ILE408 4.7 57.5 1.0 CG B:MET379 4.8 58.7 1.0 HZ B:PHE233 4.8 53.9 1.0 HD12 B:ILE408 4.8 57.5 1.0 HG22 B:VAL252 4.9 58.3 1.0 HG13 B:VAL329 4.9 54.8 1.0 HG11 B:VAL329 4.9 54.8 1.0 CD1 B:ILE408 5.0 47.9 1.0 C12 B:HUY501 5.0 87.2 1.0 HD11 B:LEU387 5.0 51.0 1.0

Fluorine binding site 3 out of 6 in the Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator


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 Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator within 5.0Å range: probe atom residue distance (Å) B Occ B:F501 b:65.2 occ:1.00 F3 B:HUY501 0.0 65.2 1.0 C16 B:HUY501 1.4 80.6 1.0 F1 B:HUY501 2.2 80.3 1.0 F2 B:HUY501 2.2 0.1 1.0 C15 B:HUY501 2.4 80.3 1.0 C14 B:HUY501 2.7 82.3 1.0 HB2 B:ALA235 2.8 45.2 1.0 HG21 B:VAL252 3.1 58.3 1.0 HB3 B:ALA235 3.3 45.2 1.0 HG22 B:VAL252 3.4 58.3 1.0 CB B:ALA235 3.4 37.6 1.0 HZ B:PHE233 3.5 53.9 1.0 HB1 B:ALA235 3.6 45.2 1.0 C17 B:HUY501 3.6 82.1 1.0 CG2 B:VAL252 3.7 48.6 1.0 HE2 B:PHE428 3.9 52.3 1.0 HZ B:PHE428 4.0 55.4 1.0 HD12 B:ILE408 4.0 57.5 1.0 C13 B:HUY501 4.1 85.0 1.0 HG23 B:VAL252 4.1 58.3 1.0 HE1 B:PHE233 4.1 54.0 1.0 CZ B:PHE233 4.2 44.9 1.0 HD21 B:LEU383 4.3 87.2 1.0 HD13 B:ILE408 4.4 57.5 1.0 HG22 B:VAL329 4.5 68.5 1.0 CE2 B:PHE428 4.5 43.6 1.0 CD1 B:ILE408 4.5 47.9 1.0 CE1 B:PHE233 4.5 45.0 1.0 CZ B:PHE428 4.5 46.2 1.0 HD11 B:ILE408 4.6 57.5 1.0 HG11 B:VAL252 4.6 62.3 1.0 C11 B:HUY501 4.7 82.7 1.0 HG21 B:VAL329 4.8 68.5 1.0 CA B:ALA235 4.8 42.0 1.0 HG13 B:VAL252 4.8 62.3 1.0 HE2 B:MET379 4.9 57.1 1.0 C12 B:HUY501 4.9 87.2 1.0 HD23 B:LEU383 5.0 87.2 1.0 CB B:VAL252 5.0 41.7 1.0

Fluorine binding site 4 out of 6 in the Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator


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 Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:92.4 occ:1.00 F1 A:HUY501 0.0 92.4 1.0 C16 A:HUY501 1.4 83.9 1.0 F2 A:HUY501 2.2 98.7 1.0 F3 A:HUY501 2.2 69.9 1.0 C15 A:HUY501 2.4 82.1 1.0 C17 A:HUY501 2.8 92.9 1.0 HB1 A:ALA235 2.9 49.6 1.0 HE2 A:MET379 2.9 54.2 1.0 HE1 A:MET379 3.2 54.2 1.0 HD11 A:LEU387 3.2 49.2 1.0 CE A:MET379 3.3 45.2 1.0 HD13 A:LEU383 3.5 87.2 1.0 CB A:ALA235 3.5 41.3 1.0 HB3 A:ALA235 3.5 49.6 1.0 HB2 A:ALA235 3.6 49.6 1.0 C14 A:HUY501 3.6 60.0 1.0 SD A:MET379 3.7 49.2 1.0 HD2 A:PHE251 3.9 47.3 1.0 C11 A:HUY501 4.2 82.3 1.0 CD1 A:LEU387 4.2 41.0 1.0 HB3 A:LEU383 4.2 57.6 1.0 HE3 A:MET379 4.3 54.2 1.0 HB2 A:PHE251 4.3 47.5 1.0 HG3 A:MET379 4.4 65.2 1.0 HD21 A:LEU387 4.4 48.0 1.0 CD2 A:PHE251 4.4 39.4 1.0 CD1 A:LEU383 4.4 72.7 1.0 HD12 A:LEU387 4.5 49.2 1.0 HG12 A:VAL329 4.5 76.1 1.0 HD12 A:LEU383 4.6 87.2 1.0 HD13 A:LEU387 4.7 49.2 1.0 CG A:MET379 4.7 54.3 1.0 C13 A:HUY501 4.8 67.3 1.0 HG11 A:VAL329 4.8 76.1 1.0 HG A:LEU387 4.9 61.5 1.0 HG22 A:VAL252 4.9 57.3 1.0 HD22 A:LEU383 4.9 70.8 1.0 CA A:ALA235 4.9 49.0 1.0 HD11 A:LEU383 5.0 87.2 1.0 CG A:PHE251 5.0 42.6 1.0 C12 A:HUY501 5.0 75.3 1.0 HE2 A:PHE251 5.0 53.1 1.0 CG1 A:VAL329 5.0 63.4 1.0 HG13 A:VAL329 5.0 76.1 1.0 CB A:PHE251 5.0 39.6 1.0

Fluorine binding site 5 out of 6 in the Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator


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 Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:98.7 occ:1.00 F2 A:HUY501 0.0 98.7 1.0 C16 A:HUY501 1.4 83.9 1.0 F3 A:HUY501 2.2 69.9 1.0 F1 A:HUY501 2.2 92.4 1.0 C15 A:HUY501 2.4 82.1 1.0 HB3 A:ALA235 2.5 49.6 1.0 C14 A:HUY501 2.8 60.0 1.0 HG22 A:VAL252 2.9 57.3 1.0 HB1 A:ALA235 3.0 49.6 1.0 CB A:ALA235 3.0 41.3 1.0 HB2 A:ALA235 3.1 49.6 1.0 HB2 A:PHE251 3.2 47.5 1.0 HG21 A:VAL252 3.5 57.3 1.0 CG2 A:VAL252 3.6 47.8 1.0 C17 A:HUY501 3.6 92.9 1.0 HG13 A:VAL252 3.8 54.8 1.0 HE2 A:PHE428 3.9 49.0 1.0 HD2 A:PHE251 4.0 47.3 1.0 HB3 A:PHE251 4.0 47.5 1.0 CB A:PHE251 4.0 39.6 1.0 C13 A:HUY501 4.1 67.3 1.0 HG11 A:VAL252 4.2 54.8 1.0 HG23 A:VAL252 4.2 57.3 1.0 CG1 A:VAL252 4.3 45.7 1.0 H A:VAL252 4.5 62.7 1.0 CA A:ALA235 4.5 49.0 1.0 CD2 A:PHE251 4.5 39.4 1.0 HE2 A:MET379 4.5 54.2 1.0 CE2 A:PHE428 4.6 40.9 1.0 CB A:VAL252 4.6 41.2 1.0 CG A:PHE251 4.6 42.6 1.0 HD11 A:LEU387 4.7 49.2 1.0 HE1 A:MET379 4.7 54.2 1.0 N A:VAL252 4.7 52.2 1.0 C11 A:HUY501 4.7 82.3 1.0 H A:ALA235 4.9 56.2 1.0 C12 A:HUY501 4.9 75.3 1.0 HD21 A:LEU387 4.9 48.0 1.0 HZ A:PHE428 5.0 45.7 1.0 C A:ALA235 5.0 45.1 1.0

Fluorine binding site 6 out of 6 in the Crystal Structure of Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator


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 Human TEAD2-Yap Binding Domain Covalently Bound to An Allosteric Regulator within 5.0Å range: probe atom residue distance (Å) B Occ A:F501 b:69.9 occ:1.00 F3 A:HUY501 0.0 69.9 1.0 C16 A:HUY501 1.4 83.9 1.0 F2 A:HUY501 2.2 98.7 1.0 F1 A:HUY501 2.2 92.4 1.0 C15 A:HUY501 2.4 82.1 1.0 C14 A:HUY501 3.2 60.0 1.0 C17 A:HUY501 3.3 92.9 1.0 HD13 A:LEU383 3.8 87.2 1.0 HE2 A:PHE428 3.8 49.0 1.0 HD21 A:LEU387 4.0 48.0 1.0 HE2 A:PHE406 4.1 60.0 1.0 CE2 A:PHE428 4.1 40.9 1.0 HD11 A:LEU387 4.2 49.2 1.0 HZ A:PHE406 4.2 69.1 1.0 HD22 A:LEU383 4.3 70.8 1.0 HD11 A:ILE408 4.3 47.8 1.0 HZ A:PHE428 4.4 45.7 1.0 C13 A:HUY501 4.4 67.3 1.0 CZ A:PHE428 4.4 38.1 1.0 HD12 A:ILE408 4.5 47.8 1.0 C11 A:HUY501 4.5 82.3 1.0 HB3 A:ALA235 4.6 49.6 1.0 HB1 A:ALA235 4.6 49.6 1.0 CD2 A:PHE428 4.7 35.4 1.0 CE2 A:PHE406 4.7 50.0 1.0 HB3 A:LEU383 4.7 57.6 1.0 CD1 A:LEU383 4.8 72.7 1.0 CZ A:PHE406 4.8 57.5 1.0 CD1 A:ILE408 4.8 39.8 1.0 HB2 A:PHE251 4.9 47.5 1.0 HD2 A:PHE428 4.9 42.4 1.0 HB2 A:ALA235 4.9 49.6 1.0 CD2 A:LEU387 4.9 40.0 1.0 HG A:LEU387 4.9 61.5 1.0 CB A:ALA235 4.9 41.3 1.0 HG22 A:VAL252 4.9 57.3 1.0 C12 A:HUY501 5.0 75.3 1.0

K.Bum-Erdene, D.Zhou, G.Gonzalez-Gutierrez, M.K.Ghozayel, Y.Si, D.Xu, H.E.Shannon, B.J.Bailey, T.W.Corson, K.E.Pollok, C.D.Wells, S.O.Meroueh. Small-Molecule Covalent Modification of Conserved Cysteine Leads to Allosteric Inhibition of the Tead⋅Yap Protein-Protein Interaction. Cell Chem Biol V. 26 378 2019.
ISSN: ESSN 2451-9448
PubMed: 30581134
DOI: 10.1016/J.CHEMBIOL.2018.11.010