Fluorine in PDB 4pjv: Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673

All present enzymatic activity of Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673:
2.4.2.30;

The structure of Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673, PDB code: 4pjv was solved by M.Aoyagi-Scharber, A.S.Gardberg, T.L.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.33 / 2.50
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	52.860, 57.740, 69.290, 77.28, 79.99, 63.88
R / Rfree (%)	21.4 / 28.7

The binding sites of Fluorine atom in the Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673 (pdb code 4pjv). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673, PDB code: 4pjv:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:12.3 occ:1.00 F2 A:2YQ601 0.0 12.3 1.0 C14 A:2YQ601 1.4 11.8 1.0 C15 A:2YQ601 2.4 11.5 1.0 C13 A:2YQ601 2.4 11.4 1.0 O A:GLY454 2.6 22.5 1.0 CB A:SER328 3.4 23.9 1.0 C16 A:2YQ601 3.6 11.3 1.0 C12 A:2YQ601 3.7 11.2 1.0 C A:GLY454 3.7 22.2 1.0 O A:HOH715 3.9 20.2 1.0 C11 A:2YQ601 4.1 11.2 1.0 CA A:SER328 4.3 22.4 1.0 CA A:GLY454 4.4 22.7 1.0 NE2 A:GLN332 4.6 22.3 1.0 O A:SER328 4.7 20.3 1.0 N A:TYR455 4.8 21.9 1.0 C A:SER328 4.9 21.1 1.0

Fluorine binding site 2 out of 4 in the Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673 within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:11.4 occ:1.00 F1 A:2YQ601 0.0 11.4 1.0 C9 A:2YQ601 1.3 11.2 1.0 C8 A:2YQ601 2.4 10.9 1.0 C10 A:2YQ601 2.4 11.1 1.0 O A:PHE463 3.2 9.8 1.0 CB A:GLU558 3.2 11.4 1.0 CE A:LYS469 3.3 11.6 1.0 C A:PHE463 3.6 9.4 1.0 C7 A:2YQ601 3.6 10.9 1.0 C1 A:2YQ601 3.7 10.8 1.0 CD A:LYS469 3.7 11.5 1.0 CB A:ALA464 3.8 9.8 1.0 CG A:LYS469 3.9 11.2 1.0 N A:ALA464 4.0 9.4 1.0 CA A:GLU558 4.0 11.4 1.0 NZ A:LYS469 4.1 12.1 1.0 CA A:ALA464 4.1 9.7 1.0 C2 A:2YQ601 4.1 10.8 1.0 O A:ASN557 4.2 12.0 1.0 CD A:GLU558 4.2 12.2 1.0 OE2 A:GLU558 4.3 12.5 1.0 CG A:GLU558 4.3 12.0 1.0 N A:PHE463 4.5 9.5 1.0 CA A:PHE463 4.5 9.2 1.0 OE1 A:GLU558 4.7 12.2 1.0 N3 A:2YQ601 4.7 11.1 1.0 CB A:LYS469 4.8 11.1 1.0 C4 A:2YQ601 4.8 10.7 1.0 CB A:TYR462 4.9 10.1 1.0 N A:GLU558 4.9 12.2 1.0

Fluorine binding site 3 out of 4 in the Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673 within 5.0Å range: probe atom residue distance (Å) B Occ B:F601 b:12.4 occ:1.00 F2 B:2YQ601 0.0 12.4 1.0 C14 B:2YQ601 1.3 11.2 1.0 C13 B:2YQ601 2.3 10.7 1.0 C15 B:2YQ601 2.4 11.0 1.0 O B:HOH741 2.8 18.9 1.0 O B:GLY454 3.0 26.3 1.0 OG B:SER328 3.1 34.9 1.0 CB B:SER328 3.4 33.4 1.0 C12 B:2YQ601 3.6 10.3 1.0 C16 B:2YQ601 3.6 10.7 1.0 NE2 B:GLN332 3.9 33.4 1.0 C B:GLY454 4.1 26.8 1.0 C11 B:2YQ601 4.1 10.3 1.0 CA B:SER328 4.5 32.4 1.0 CA B:GLY454 4.7 27.9 1.0 O B:SER328 4.8 30.2 1.0 C19 B:2YQ601 5.0 10.0 1.0

Fluorine binding site 4 out of 4 in the Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of PARP2 Catalytic Domain Bound to Inhibitor Bmn 673 within 5.0Å range: probe atom residue distance (Å) B Occ B:F601 b:10.6 occ:1.00 F1 B:2YQ601 0.0 10.6 1.0 C9 B:2YQ601 1.3 10.4 1.0 C10 B:2YQ601 2.3 10.1 1.0 C8 B:2YQ601 2.4 10.1 1.0 O B:PHE463 3.2 8.5 1.0 CB B:ALA464 3.5 8.5 1.0 C B:PHE463 3.5 8.1 1.0 C1 B:2YQ601 3.6 10.0 1.0 CE B:LYS469 3.6 11.2 1.0 CB B:GLU558 3.6 10.5 1.0 C7 B:2YQ601 3.6 10.1 1.0 N B:ALA464 3.8 8.0 1.0 CD B:LYS469 3.8 10.9 1.0 CG B:LYS469 3.9 10.4 1.0 CA B:ALA464 3.9 8.4 1.0 C2 B:2YQ601 4.1 10.0 1.0 N B:PHE463 4.4 8.0 1.0 NZ B:LYS469 4.4 11.8 1.0 CA B:GLU558 4.4 10.6 1.0 CA B:PHE463 4.4 7.8 1.0 CD B:GLU558 4.5 11.5 1.0 OE2 B:GLU558 4.6 11.8 1.0 O B:ASN557 4.7 11.6 1.0 C4 B:2YQ601 4.7 10.2 1.0 CG B:GLU558 4.7 11.3 1.0 OG B:SER470 4.7 8.9 1.0 CB B:LYS469 4.8 10.2 1.0 N3 B:2YQ601 4.8 10.1 1.0 OE1 B:GLU558 4.8 11.3 1.0 CB B:TYR462 4.8 8.9 1.0 O B:2YQ601 4.8 9.7 1.0 C B:TYR462 5.0 8.1 1.0

M.Aoyagi-Scharber, A.S.Gardberg, B.K.Yip, B.Wang, Y.Shen, P.A.Fitzpatrick. Structural Basis For the Inhibition of Poly(Adp-Ribose) Polymerases 1 and 2 By Bmn 673, A Potent Inhibitor Derived From Dihydropyridophthalazinone. Acta Crystallogr.,Sect.F V. 70 1143 2014.
ISSN: ESSN 2053-230X
PubMed: 25195882
DOI: 10.1107/S2053230X14015088