Atomistry » Fluorine » PDB 8hf8-8hxf » 8hkn
Atomistry »
  Fluorine »
    PDB 8hf8-8hxf »
      8hkn »

Fluorine in PDB 8hkn: Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib

Enzymatic activity of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib

All present enzymatic activity of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib:
2.4.2.30;

Protein crystallography data

The structure of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib, PDB code: 8hkn was solved by X.Y.Wang, J.Zhou, B.L.Xu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.98 / 2.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.01, 85.584, 95.413, 90, 90.03, 90
R / Rfree (%) 18.2 / 26.1

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib (pdb code 8hkn). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 8 binding sites of Fluorine where determined in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib, PDB code: 8hkn:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Fluorine binding site 1 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 1 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F602

b:43.1
occ:1.00
 F01 B:25I602 0.0 43.1 1.0
C15 B:25I602 1.3 39.2 1.0
F03 B:25I602 2.2 44.6 1.0
F02 B:25I602 2.2 45.1 1.0
C14 B:25I602 2.3 35.1 1.0
N03 B:25I602 2.7 29.8 1.0
OH B:TYR279 3.0 26.7 1.0
O B:HOH707 3.3 33.1 1.0
N04 B:25I602 3.4 34.0 1.0
O B:HOH748 3.6 27.2 1.0
O B:HOH745 3.7 40.4 1.0
O B:HOH761 3.7 38.4 1.0
C13 B:25I602 3.9 28.8 1.0
CB B:GLU335 3.9 29.3 1.0
CG B:GLU335 4.0 34.3 1.0
CA B:GLU335 4.1 28.5 1.0
N02 B:25I602 4.2 29.1 1.0
CZ B:TYR279 4.2 27.2 1.0
CD B:PRO447 4.3 33.2 1.0
CA B:ALA446 4.5 29.1 1.0
CD B:GLU335 4.6 39.2 1.0
OE1 B:GLU335 4.8 42.3 1.0
CB B:ALA446 4.8 28.9 1.0
N B:GLU335 4.9 27.1 1.0
CE1 B:TYR279 5.0 26.1 1.0

Fluorine binding site 2 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 2 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F602

b:45.1
occ:1.00
 F02 B:25I602 0.0 45.1 1.0
C15 B:25I602 1.3 39.2 1.0
F03 B:25I602 2.1 44.6 1.0
F01 B:25I602 2.2 43.1 1.0
C14 B:25I602 2.3 35.1 1.0
O B:HOH761 2.6 38.4 1.0
N04 B:25I602 2.7 34.0 1.0
NH2 B:ARG444 3.2 50.2 1.0
N03 B:25I602 3.5 29.8 1.0
CZ B:ARG444 3.7 47.7 1.0
N02 B:25I602 3.9 29.1 1.0
O B:HOH745 4.1 40.4 1.0
NE B:ARG444 4.1 47.3 1.0
CG B:GLU335 4.2 34.3 1.0
NH1 B:ARG444 4.3 47.7 1.0
O B:HOH792 4.3 33.4 1.0
C13 B:25I602 4.3 28.8 1.0
CB B:ARG444 4.5 37.2 1.0
O B:HOH740 4.6 50.3 1.0
OH B:TYR279 4.7 26.7 1.0
CB B:GLU335 4.8 29.3 1.0
CA B:GLU335 4.8 28.5 1.0
O B:HOH768 4.9 39.4 1.0
O B:GLU335 4.9 23.9 1.0
CD B:GLU335 4.9 39.2 1.0

Fluorine binding site 3 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 3 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F602

b:44.6
occ:1.00
 F03 B:25I602 0.0 44.6 1.0
C15 B:25I602 1.3 39.2 1.0
F02 B:25I602 2.1 45.1 1.0
F01 B:25I602 2.2 43.1 1.0
C14 B:25I602 2.4 35.1 1.0
N03 B:25I602 3.2 29.8 1.0
N04 B:25I602 3.2 34.0 1.0
O B:HOH768 3.4 39.4 1.0
CA B:ALA446 3.6 29.1 1.0
O B:ILE445 3.7 32.3 1.0
CD B:PRO447 3.8 33.2 1.0
N B:ALA446 3.9 29.6 1.0
C B:ILE445 3.9 31.5 1.0
C13 B:25I602 4.2 28.8 1.0
N02 B:25I602 4.2 29.1 1.0
CB B:ARG444 4.3 37.2 1.0
N B:PRO447 4.4 29.2 1.0
C B:ALA446 4.4 30.3 1.0
O B:HOH761 4.5 38.4 1.0
CB B:ALA446 4.5 28.9 1.0
OH B:TYR279 4.5 26.7 1.0
O B:ARG444 4.6 27.1 1.0
C B:ARG444 4.7 31.4 1.0
CZ B:ARG444 4.7 47.7 1.0
NH2 B:ARG444 4.8 50.2 1.0
O B:HOH745 4.8 40.4 1.0
NH1 B:ARG444 4.9 47.7 1.0
CG B:PRO447 4.9 31.8 1.0
N B:ILE445 4.9 29.6 1.0
NE B:ARG444 5.0 47.3 1.0

Fluorine binding site 4 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 4 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F602

b:28.6
occ:1.00
 F04 B:25I602 0.0 28.6 1.0
C16 B:25I602 1.4 28.1 1.0
C17 B:25I602 2.4 28.6 1.0
C08 B:25I602 2.4 25.3 1.0
C10 B:25I602 2.8 27.7 1.0
C09 B:25I602 3.0 24.8 1.0
N01 B:25I602 3.1 25.0 1.0
CE1 B:TYR462 3.2 28.4 1.0
O B:GLY460 3.2 26.4 1.0
CD1 B:TYR462 3.3 26.8 1.0
CD2 B:TYR455 3.4 26.3 1.0
O B:HOH735 3.6 32.8 1.0
C07 B:25I602 3.7 26.9 1.0
C18 B:25I602 3.7 27.1 1.0
CE2 B:TYR455 3.8 25.6 1.0
O02 B:25I602 4.0 22.5 1.0
CZ B:TYR462 4.1 29.8 1.0
O3 B:GOL601 4.1 56.9 1.0
C06 B:25I602 4.2 25.4 1.0
C13 B:25I602 4.2 28.8 1.0
C B:GLY460 4.3 23.6 1.0
CG B:TYR462 4.3 25.6 1.0
C11 B:25I602 4.3 26.6 1.0
N B:GLY460 4.5 25.7 1.0
CG B:TYR455 4.6 27.9 1.0
O B:GLY458 4.6 23.4 1.0
OH B:TYR462 4.7 30.6 1.0
C3 B:GOL601 4.9 62.1 1.0
CE2 B:TYR462 4.9 27.4 1.0
CD2 B:TYR462 4.9 26.1 1.0
N03 B:25I602 5.0 29.8 1.0
C1 B:GOL601 5.0 60.7 1.0

Fluorine binding site 5 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 5 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F602

b:44.8
occ:1.00
 F01 A:25I602 0.0 44.8 1.0
C15 A:25I602 1.3 39.8 1.0
F02 A:25I602 2.1 38.1 1.0
F03 A:25I602 2.2 42.6 1.0
C14 A:25I602 2.4 35.1 1.0
N04 A:25I602 2.8 34.7 1.0
NH2 A:ARG444 3.3 47.1 1.0
CZ A:ARG444 3.3 52.5 1.0
NH1 A:ARG444 3.4 45.0 1.0
N03 A:25I602 3.6 29.7 1.0
N02 A:25I602 4.0 31.2 1.0
NE A:ARG444 4.0 46.5 1.0
O A:HOH784 4.1 46.5 1.0
C3 A:GOL601 4.1 77.8 1.0
O A:HOH743 4.2 49.5 1.0
O A:HOH704 4.2 35.1 1.0
O3 A:GOL601 4.3 57.7 1.0
CB A:ARG444 4.3 32.4 1.0
C13 A:25I602 4.4 30.4 1.0
O A:HOH812 4.4 51.2 1.0
CD A:ARG444 4.7 40.3 1.0
O A:HOH758 4.9 38.7 1.0
O A:ILE445 4.9 32.9 1.0
OH A:TYR279 5.0 37.4 1.0

Fluorine binding site 6 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 6 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F602

b:38.1
occ:1.00
 F02 A:25I602 0.0 38.1 1.0
C15 A:25I602 1.3 39.8 1.0
F01 A:25I602 2.1 44.8 1.0
F03 A:25I602 2.2 42.6 1.0
C14 A:25I602 2.3 35.1 1.0
N03 A:25I602 3.1 29.7 1.0
N04 A:25I602 3.1 34.7 1.0
O A:ILE445 3.2 32.9 1.0
O A:HOH784 3.4 46.5 1.0
CA A:ALA446 3.4 25.6 1.0
C A:ILE445 3.7 30.6 1.0
N A:ALA446 3.8 25.6 1.0
CD A:PRO447 4.0 28.1 1.0
N02 A:25I602 4.1 31.2 1.0
C13 A:25I602 4.1 30.4 1.0
O A:HOH812 4.1 51.2 1.0
CB A:ARG444 4.2 32.4 1.0
C A:ALA446 4.2 28.6 1.0
NH1 A:ARG444 4.3 45.0 1.0
O A:ARG444 4.4 28.6 1.0
N A:PRO447 4.4 27.4 1.0
CB A:ALA446 4.4 27.9 1.0
C A:ARG444 4.5 30.8 1.0
CZ A:ARG444 4.6 52.5 1.0
O A:HOH719 4.7 29.5 1.0
OH A:TYR279 4.8 37.4 1.0
N A:ILE445 4.8 31.6 1.0
CA A:ILE445 4.9 31.8 1.0
O A:HOH743 4.9 49.5 1.0
CA A:ARG444 5.0 30.2 1.0

Fluorine binding site 7 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 7 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F602

b:42.6
occ:1.00
 F03 A:25I602 0.0 42.6 1.0
C15 A:25I602 1.4 39.8 1.0
F01 A:25I602 2.2 44.8 1.0
F02 A:25I602 2.2 38.1 1.0
C14 A:25I602 2.4 35.1 1.0
N03 A:25I602 2.9 29.7 1.0
OH A:TYR279 2.9 37.4 1.0
O A:HOH743 3.2 49.5 1.0
O A:HOH719 3.5 29.5 1.0
N04 A:25I602 3.6 34.7 1.0
CG A:GLU335 3.8 38.6 1.0
CZ A:TYR279 4.1 36.6 1.0
O A:HOH812 4.1 51.2 1.0
C13 A:25I602 4.1 30.4 1.0
CA A:GLU335 4.2 29.6 1.0
CD A:PRO447 4.3 28.1 1.0
CB A:GLU335 4.3 33.2 1.0
N02 A:25I602 4.4 31.2 1.0
CA A:ALA446 4.6 25.6 1.0
CE2 A:TYR279 4.7 34.2 1.0
C3 A:GOL601 4.8 77.8 1.0
CD A:GLU335 4.8 41.1 1.0
N A:GLU335 4.8 29.9 1.0
CB A:ALA446 4.9 27.9 1.0
OE2 A:GLU335 5.0 35.9 1.0

Fluorine binding site 8 out of 8 in 8hkn

Go back to Fluorine Binding Sites List in 8hkn
Fluorine binding site 8 out of 8 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F602

b:25.6
occ:1.00
 F04 A:25I602 0.0 25.6 1.0
C16 A:25I602 1.4 29.0 1.0
C08 A:25I602 2.4 29.6 1.0
C17 A:25I602 2.4 26.8 1.0
C09 A:25I602 2.9 30.4 1.0
C10 A:25I602 2.9 26.4 1.0
CE1 A:TYR462 3.1 30.9 1.0
N01 A:25I602 3.1 26.0 1.0
CD1 A:TYR462 3.2 29.1 1.0
O A:GLY460 3.2 23.1 1.0
C07 A:25I602 3.6 29.8 1.0
CD2 A:TYR455 3.6 28.9 1.0
C18 A:25I602 3.6 25.8 1.0
O02 A:25I602 3.8 30.4 1.0
CE2 A:TYR455 3.9 27.7 1.0
CZ A:TYR462 4.0 29.7 1.0
C06 A:25I602 4.1 29.0 1.0
CG A:TYR462 4.2 29.8 1.0
C A:GLY460 4.2 26.4 1.0
C13 A:25I602 4.3 30.4 1.0
C11 A:25I602 4.4 28.2 1.0
N A:GLY460 4.5 26.8 1.0
O A:GLY458 4.6 23.8 1.0
OH A:TYR462 4.6 32.3 1.0
OE2 A:GLU335 4.8 35.9 1.0
CG A:TYR455 4.8 29.6 1.0
CE2 A:TYR462 4.8 29.8 1.0
CD2 A:TYR462 4.9 29.0 1.0
CB A:TYR462 4.9 27.3 1.0

Reference:

X.Y.Wang, J.Zhou, B.L.Xu. Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Approved Drug Fluzoparib To Be Published.
Page generated: Wed Jul 16 05:15:19 2025

Last articles

Fe in 1DV6
Fe in 1DV3
Fe in 1DUO
Fe in 1DUK
Fe in 1DT0
Fe in 1DTM
Fe in 1DTI
Fe in 1DTG
Fe in 1DT6
Fe in 1DT1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy