Fluorine in PDB 8he8: Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor

All present enzymatic activity of Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor:
2.4.2.30;

The structure of Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor, PDB code: 8he8 was solved by X.Y.Wang, B.L.Xu, J.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.09 / 3.05
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.113, 103.362, 134.925, 90, 92.04, 90
R / Rfree (%)	20.7 / 25.6

The binding sites of Fluorine atom in the Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor (pdb code 8he8). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor, PDB code: 8he8:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F602 b:35.7 occ:1.00 F01 A:1WI602 0.0 35.7 1.0 C13 A:1WI602 1.4 31.6 1.0 C12 A:1WI602 2.4 32.8 1.0 C14 A:1WI602 2.4 30.3 1.0 C16 A:1WI602 3.0 28.7 1.0 C17 A:1WI602 3.0 35.8 1.0 O A:GLY460 3.0 27.4 1.0 N03 A:1WI602 3.2 29.4 1.0 CD2 A:TYR455 3.4 42.7 1.0 CD1 A:TYR462 3.5 38.0 1.0 CE1 A:TYR462 3.6 35.2 1.0 C11 A:1WI602 3.6 36.7 1.0 C15 A:1WI602 3.7 32.3 1.0 CE2 A:TYR455 3.7 39.0 1.0 O03 A:1WI602 3.9 33.6 1.0 C10 A:1WI602 4.1 34.4 1.0 C A:GLY460 4.1 32.1 1.0 CG A:TYR462 4.3 31.2 1.0 C20 A:1WI602 4.4 30.4 1.0 C18 A:1WI602 4.4 38.2 1.0 CZ A:TYR462 4.4 37.8 1.0 N A:GLY460 4.5 37.4 1.0 CG A:TYR455 4.7 41.3 1.0 O A:GLY458 4.8 35.2 1.0 N A:TYR462 4.9 31.1 1.0 CB A:TYR462 4.9 28.8 1.0 CA A:GLY460 4.9 38.2 1.0

Fluorine binding site 2 out of 3 in the Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:F602 b:39.9 occ:1.00 F01 B:1WI602 0.0 39.9 1.0 C13 B:1WI602 1.4 42.6 1.0 C12 B:1WI602 2.4 45.6 1.0 C14 B:1WI602 2.4 38.4 1.0 O B:GLY460 2.8 40.5 1.0 C16 B:1WI602 2.9 33.5 1.0 C17 B:1WI602 3.1 35.1 1.0 N03 B:1WI602 3.2 29.8 1.0 CD1 B:TYR462 3.4 43.5 1.0 CE1 B:TYR462 3.5 42.0 1.0 C15 B:1WI602 3.6 37.6 1.0 C11 B:1WI602 3.6 45.9 1.0 O03 B:1WI602 3.8 33.3 1.0 CD2 B:TYR455 3.9 48.9 1.0 C B:GLY460 3.9 40.6 1.0 CE2 B:TYR455 4.1 38.2 1.0 C10 B:1WI602 4.1 39.6 1.0 O3 B:GOL601 4.2 49.6 1.0 CG B:TYR462 4.3 43.7 1.0 N B:GLY460 4.3 40.1 1.0 C20 B:1WI602 4.4 31.8 1.0 CZ B:TYR462 4.4 43.2 1.0 C18 B:1WI602 4.5 35.5 1.0 C3 B:GOL601 4.6 43.4 1.0 CA B:GLY460 4.7 36.5 1.0 N B:ILE461 4.7 33.1 1.0 CA B:ILE461 4.8 36.1 1.0 N B:TYR462 4.8 36.8 1.0 CB B:TYR462 4.9 38.2 1.0 O B:GLY458 5.0 38.0 1.0

Fluorine binding site 3 out of 3 in the Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to A Quinazoline-2,4(1H,3H)-Dione Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ C:F601 b:54.0 occ:1.00 F01 C:1WI601 0.0 54.0 1.0 C13 C:1WI601 1.4 52.3 1.0 C14 C:1WI601 2.4 49.9 1.0 C12 C:1WI601 2.4 51.6 1.0 C16 C:1WI601 2.9 50.9 1.0 O C:GLY460 3.0 52.3 1.0 CD1 C:TYR462 3.3 52.4 1.0 N03 C:1WI601 3.3 54.3 1.0 C17 C:1WI601 3.4 53.4 1.0 CE1 C:TYR462 3.4 53.0 1.0 O03 C:1WI601 3.6 57.9 1.0 C15 C:1WI601 3.6 51.5 1.0 C11 C:1WI601 3.6 48.1 1.0 CD2 C:TYR455 3.7 69.9 1.0 CE2 C:TYR455 4.0 71.4 1.0 C C:GLY460 4.1 54.7 1.0 C10 C:1WI601 4.1 48.2 1.0 CG C:TYR462 4.2 51.6 1.0 CZ C:TYR462 4.4 52.3 1.0 C20 C:1WI601 4.4 53.8 1.0 N C:GLY460 4.5 53.6 1.0 N C:TYR462 4.8 48.0 1.0 O C:GLY458 4.8 56.1 1.0 C18 C:1WI601 4.9 49.4 1.0 CG C:TYR455 4.9 70.6 1.0 N C:ILE461 4.9 55.3 1.0 CA C:GLY460 4.9 56.0 1.0 CB C:TYR462 4.9 51.7 1.0 CA C:ILE461 4.9 52.9 1.0

J.Zhou, T.Du, X.Wang, H.Yao, J.Deng, Y.Li, X.Chen, L.Sheng, M.Ji, B.Xu. Discovery of Quinazoline-2,4(1 H ,3 H )-Dione Derivatives Containing A Piperizinone Moiety As Potent Parp-1/2 Inhibitors─Design, Synthesis, in Vivo Antitumor Activity, and X-Ray Crystal Structure Analysis. J.Med.Chem. V. 66 14095 2023.
ISSN: ISSN 0022-2623
PubMed: 37843892
DOI: 10.1021/ACS.JMEDCHEM.3C01152