Fluorine in PDB 6hr2: Crystal Structure of Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb

The structure of Crystal Structure of Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb, PDB code: 6hr2 was solved by M.Roy, G.Bader, E.Diers, N.Trainor, W.Farnaby, A.Ciulli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.80 / 1.76
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	60.332, 61.678, 81.603, 69.43, 83.38, 86.42
R / Rfree (%)	21.6 / 23.6

The binding sites of Fluorine atom in the Crystal Structure of Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb (pdb code 6hr2). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb, PDB code: 6hr2:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb


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 Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb within 5.0Å range: probe atom residue distance (Å) B Occ B:F301 b:34.0 occ:1.00 F34 B:FWZ301 0.0 34.0 1.0 C32 B:FWZ301 1.4 34.4 1.0 H1 B:FWZ301 2.2 34.5 0.0 C35 B:FWZ301 2.4 34.1 1.0 C36 B:FWZ301 2.4 32.4 1.0 C31 B:FWZ301 2.4 34.5 1.0 HA A:ASN1540 2.5 29.7 0.0 H30 B:FWZ301 2.6 34.1 0.0 H31 B:FWZ301 2.6 32.4 0.0 N1 B:FWZ301 2.7 34.5 1.0 OH B:TYR112 3.3 34.3 1.0 O A:PHE1539 3.3 32.3 1.0 H29 B:FWZ301 3.4 34.1 0.0 H32 B:FWZ301 3.4 32.4 0.0 HE2 A:PHE1539 3.4 34.3 0.0 CE2 A:PHE1539 3.4 34.4 1.0 OD1 A:ASN1540 3.4 31.6 1.0 HH B:TYR112 3.6 34.3 0.0 O33 B:FWZ301 3.6 31.6 1.0 CA A:ASN1540 3.6 29.7 1.0 H9 B:FWZ301 3.6 31.6 0.0 CD2 A:PHE1539 3.6 31.7 1.0 CZ B:TYR112 3.7 33.5 1.0 HD2 A:PHE1539 3.7 31.6 0.0 C A:PHE1539 3.9 31.6 1.0 CZ A:PHE1539 4.0 32.2 1.0 CG A:ASN1540 4.1 46.5 1.0 C2 B:FWZ301 4.1 33.0 1.0 N A:ASN1540 4.1 28.8 1.0 H50 B:FWZ301 4.2 30.4 0.0 CE1 B:TYR112 4.2 26.7 1.0 CE2 B:TYR112 4.2 27.9 1.0 H6 B:FWZ301 4.2 32.5 0.0 CB A:ASN1540 4.3 27.7 1.0 O A:HOH1601 4.3 34.3 1.0 HH22 B:ARG69 4.3 29.7 0.0 HE1 B:TYR112 4.3 26.7 0.0 O A:ASN1540 4.3 33.1 1.0 O9 B:FWZ301 4.3 32.9 1.0 HE2 B:TYR112 4.3 27.9 0.0 CG A:PHE1539 4.3 30.5 1.0 HB3 A:ASN1540 4.4 27.7 0.0 HZ A:PHE1539 4.4 32.2 0.0 C A:ASN1540 4.4 34.0 1.0 C7 B:FWZ301 4.5 31.6 1.0 CE1 A:PHE1539 4.6 33.8 1.0 C4 B:FWZ301 4.7 32.5 1.0 H17 B:FWZ301 4.7 33.1 0.0 HH21 B:ARG69 4.8 30.0 0.0 C3 B:FWZ301 4.8 33.5 1.0 H8 B:FWZ301 4.8 31.7 0.0 CD1 A:PHE1539 4.8 32.9 1.0 NH2 B:ARG69 4.9 29.8 1.0 H A:ASN1540 5.0 28.8 0.0 C6 B:FWZ301 5.0 32.5 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb


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 Protac 2 in Complex with the Bromodomain of Human SMARCA4 and Pvhl:Elonginc:Elonginb within 5.0Å range: probe atom residue distance (Å) B Occ F:F301 b:27.6 occ:1.00 F34 F:FWZ301 0.0 27.6 1.0 C32 F:FWZ301 1.4 26.0 1.0 H1 F:FWZ301 2.2 24.1 0.0 C31 F:FWZ301 2.4 25.5 1.0 C36 F:FWZ301 2.4 23.9 1.0 C35 F:FWZ301 2.4 23.7 1.0 HA E:ASN1540 2.5 24.4 0.0 N1 F:FWZ301 2.6 24.1 1.0 H31 F:FWZ301 2.6 23.8 0.0 H30 F:FWZ301 2.6 23.7 0.0 HE2 E:PHE1539 3.2 30.8 0.0 CE2 E:PHE1539 3.2 30.8 1.0 O E:PHE1539 3.3 26.3 1.0 OH F:TYR112 3.3 27.1 1.0 OD1 E:ASN1540 3.4 26.5 1.0 H32 F:FWZ301 3.4 23.9 0.0 H29 F:FWZ301 3.4 23.8 0.0 CD2 E:PHE1539 3.4 27.8 1.0 O33 F:FWZ301 3.5 24.9 1.0 H9 F:FWZ301 3.6 27.7 0.0 HD2 E:PHE1539 3.6 27.8 0.0 CA E:ASN1540 3.6 24.3 1.0 HH F:TYR112 3.6 27.1 0.0 CZ F:TYR112 3.7 26.6 1.0 CZ E:PHE1539 3.8 29.0 1.0 C E:PHE1539 3.8 27.6 1.0 CG E:ASN1540 4.0 39.1 1.0 N E:ASN1540 4.1 25.2 1.0 C2 F:FWZ301 4.1 24.6 1.0 H50 F:FWZ301 4.1 29.8 0.0 CE1 F:TYR112 4.2 23.3 1.0 O E:HOH1701 4.2 27.6 1.0 CG E:PHE1539 4.2 26.3 1.0 HZ E:PHE1539 4.2 29.0 0.0 HE1 F:TYR112 4.2 23.2 0.0 H6 F:FWZ301 4.3 28.7 0.0 O9 F:FWZ301 4.3 24.5 1.0 CB E:ASN1540 4.3 24.1 1.0 CE2 F:TYR112 4.3 23.9 1.0 HB3 E:ASN1540 4.4 24.1 0.0 O E:ASN1540 4.4 26.1 1.0 HH22 F:ARG69 4.5 31.6 0.0 C E:ASN1540 4.5 27.7 1.0 C7 F:FWZ301 4.5 27.6 1.0 CE1 E:PHE1539 4.5 29.9 1.0 HE2 F:TYR112 4.5 23.9 0.0 C4 F:FWZ301 4.6 23.9 1.0 CD1 E:PHE1539 4.6 28.9 1.0 HE1 F:HIS110 4.7 29.7 0.0 H17 F:FWZ301 4.7 24.6 0.0 H8 F:FWZ301 4.8 27.6 0.0 C3 F:FWZ301 4.8 29.4 1.0 HH21 F:ARG69 4.8 31.7 0.0 H E:ASN1540 4.9 25.2 0.0 ND2 E:ASN1540 5.0 31.3 1.0 CA E:PHE1539 5.0 24.2 1.0

W.Farnaby, M.Koegl, M.J.Roy, C.Whitworth, E.Diers, N.Trainor, D.Zollman, S.Steurer, J.Karolyi-Oezguer, C.Riedmueller, T.Gmaschitz, J.Wachter, C.Dank, M.Galant, B.Sharps, K.Rumpel, E.Traxler, T.Gerstberger, R.Schnitzer, O.Petermann, P.Greb, H.Weinstabl, G.Bader, A.Zoephel, A.Weiss-Puxbaum, K.Ehrenhofer-Wolfer, S.Wohrle, G.Boehmelt, J.Rinnenthal, H.Arnhof, N.Wiechens, M.Y.Wu, T.Owen-Hughes, P.Ettmayer, M.Pearson, D.B.Mcconnell, A.Ciulli. Baf Complex Vulnerabilities in Cancer Demonstrated Via Structure-Based Protac Design. Nat.Chem.Biol. V. 15 672 2019.
ISSN: ESSN 1552-4469
PubMed: 31178587
DOI: 10.1038/S41589-019-0294-6