Fluorine in PDB 4hhy: Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors

All present enzymatic activity of Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors:
2.4.2.30;

The structure of Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors, PDB code: 4hhy was solved by Q.F.Liu, T.T.Chen, Y.C.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.61 / 2.36
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	103.797, 107.549, 143.107, 90.00, 90.00, 90.00
R / Rfree (%)	23.7 / 29.9

The binding sites of Fluorine atom in the Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors (pdb code 4hhy). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors, PDB code: 4hhy:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors


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 Parp Catalytic Domain in Complex with Novel Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:F401 b:36.5 occ:1.00 FAE A:15R401 0.0 36.5 1.0 CBE A:15R401 1.3 27.1 1.0 CAL A:15R401 2.2 24.2 1.0 CBH A:15R401 2.4 24.0 1.0 CAT A:15R401 2.7 13.7 1.0 CBB A:15R401 3.1 27.4 1.0 CE2 A:TYR228 3.2 12.2 1.0 NBP A:15R401 3.2 14.2 1.0 CB A:ALA219 3.3 7.1 1.0 OH A:TYR228 3.3 13.1 1.0 CAQ A:15R401 3.5 7.7 1.0 CAK A:15R401 3.5 21.2 1.0 CAO A:15R401 3.6 20.7 1.0 CZ A:TYR228 3.7 14.3 1.0 N A:ALA219 3.9 4.6 1.0 CA A:ALA219 3.9 5.6 1.0 CBD A:15R401 4.0 20.8 1.0 OAB A:15R401 4.2 22.2 1.0 CD2 A:TYR228 4.4 10.0 1.0 CBN A:15R401 4.4 6.3 1.0 CAU A:15R401 4.7 2.1 1.0

Fluorine binding site 2 out of 4 in the Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors


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 Parp Catalytic Domain in Complex with Novel Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:F401 b:19.8 occ:1.00 FAE B:15R401 0.0 19.8 1.0 CBE B:15R401 1.3 19.9 1.0 CBH B:15R401 2.3 19.0 1.0 CAL B:15R401 2.3 15.1 1.0 CBB B:15R401 2.7 21.0 1.0 O B:HOH510 3.1 11.5 1.0 CB B:ALA219 3.1 12.6 1.0 O B:HOH509 3.3 4.5 1.0 OAB B:15R401 3.3 12.4 1.0 NBP B:15R401 3.3 16.4 1.0 CAO B:15R401 3.5 14.7 1.0 CAK B:15R401 3.6 16.2 1.0 CAT B:15R401 3.6 16.2 1.0 CA B:ALA219 3.7 12.9 1.0 CBD B:15R401 4.0 17.5 1.0 N B:ALA219 4.3 12.8 1.0 CAU B:15R401 4.4 16.5 1.0 CB B:ALA223 4.6 11.9 1.0 CD B:PRO220 4.7 11.9 1.0 OH B:TYR49 4.9 3.8 1.0 CB B:ASP105 4.9 4.3 1.0 C B:ALA219 4.9 12.8 1.0

Fluorine binding site 3 out of 4 in the Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors


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 Parp Catalytic Domain in Complex with Novel Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ C:F401 b:45.8 occ:1.00 FAE C:15R401 0.0 45.8 1.0 CBE C:15R401 1.3 42.7 1.0 CAL C:15R401 2.3 33.9 1.0 CBH C:15R401 2.3 34.4 1.0 CBB C:15R401 2.9 42.9 1.0 CAT C:15R401 2.9 33.9 1.0 NBP C:15R401 3.1 46.5 1.0 CB C:ALA219 3.4 21.7 1.0 CAQ C:15R401 3.5 31.9 1.0 CAO C:15R401 3.6 31.9 1.0 CAK C:15R401 3.6 27.2 1.0 N C:ALA219 3.7 18.6 1.0 OH C:TYR228 3.8 61.8 1.0 OAB C:15R401 3.8 27.5 1.0 CA C:ALA219 3.9 19.8 1.0 CBD C:15R401 4.1 36.9 1.0 CZ C:TYR228 4.4 52.3 1.0 CAU C:15R401 4.4 21.2 1.0 CE2 C:TYR228 4.6 52.8 1.0 O C:GLY233 4.6 10.5 1.0 C C:ILE218 4.7 14.8 1.0 CBN C:15R401 4.9 20.9 1.0

Fluorine binding site 4 out of 4 in the Crystal Structure of Parp Catalytic Domain in Complex with Novel Inhibitors


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 Parp Catalytic Domain in Complex with Novel Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ D:F401 b:50.3 occ:1.00 FAE D:15R401 0.0 50.3 1.0 CBE D:15R401 1.3 54.0 1.0 CAL D:15R401 2.3 50.1 1.0 CBH D:15R401 2.3 48.2 1.0 CAT D:15R401 2.7 44.3 1.0 CBB D:15R401 2.9 43.4 1.0 CB D:ALA219 3.0 30.6 1.0 NBP D:15R401 3.1 37.5 1.0 N D:ALA219 3.2 23.9 1.0 CA D:ALA219 3.4 21.8 1.0 OH D:TYR228 3.4 38.3 1.0 CE2 D:TYR228 3.4 49.4 1.0 CAK D:15R401 3.5 56.1 1.0 CAO D:15R401 3.6 48.9 1.0 CZ D:TYR228 3.8 49.3 1.0 CAQ D:15R401 3.9 44.5 1.0 OAB D:15R401 4.0 32.8 1.0 CBD D:15R401 4.0 58.9 1.0 C D:ILE218 4.1 24.9 1.0 O D:ARG217 4.2 25.9 1.0 CAU D:15R401 4.4 23.1 1.0 O D:GLY233 4.5 7.2 1.0 CD2 D:TYR228 4.5 39.9 1.0 CA D:ILE218 4.6 23.6 1.0 O D:ILE218 4.8 19.0 1.0 C D:ALA219 4.9 22.4 1.0

N.Ye, C.H.Chen, T.Chen, Z.Song, J.X.He, X.J.Huan, S.S.Song, Q.Liu, Y.Chen, J.Ding, Y.Xu, Z.H.Miao, A.Zhang. Design, Synthesis, and Biological Evaluation of A Series of Benzo[De][1,7]Naphthyridin-7(8H)-Ones Bearing A Functionalized Longer Chain Appendage As Novel PARP1 Inhibitors. J.Med.Chem. V. 56 2885 2013.
ISSN: ISSN 0022-2623
PubMed: 23473053
DOI: 10.1021/JM301825T