Fluorine in PDB 8hks: Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290)

Enzymatic activity of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290)

All present enzymatic activity of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290):
2.4.2.30;

Protein crystallography data

The structure of Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290), PDB code: 8hks 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) 95.77 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 81.006, 86.333, 103.619, 90, 112.44, 90
R / Rfree (%) 18.1 / 23.8

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290) (pdb code 8hks). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290), PDB code: 8hks:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 8hks

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Fluorine binding site 1 out of 4 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290)


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 Pamiparib(Bgb-290) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F603

b:26.3
occ:1.00
 F A:DS9603 0.0 26.3 1.0
C10 A:DS9603 1.3 23.3 1.0
C11 A:DS9603 2.3 19.1 1.0
C9 A:DS9603 2.3 20.7 1.0
CB A:ALA464 3.1 19.6 1.0
O A:PHE463 3.2 23.6 1.0
CG A:GLU558 3.4 26.7 1.0
C A:PHE463 3.4 24.5 1.0
C12 A:DS9603 3.6 22.1 1.0
N A:ALA464 3.6 23.3 1.0
CA A:ALA464 3.6 26.7 1.0
C8 A:DS9603 3.6 24.9 1.0
CE A:LYS469 3.7 23.8 1.0
CD A:LYS469 3.9 23.7 1.0
C15 A:DS9603 4.1 24.2 1.0
CG A:LYS469 4.1 21.6 1.0
O A:ASN557 4.2 30.5 1.0
NZ A:LYS469 4.3 30.1 1.0
CD A:GLU558 4.4 29.2 1.0
CA A:PHE463 4.4 25.2 1.0
CA A:GLU558 4.4 21.2 1.0
CB A:GLU558 4.4 19.7 1.0
N A:PHE463 4.5 21.0 1.0
OE2 A:GLU558 4.7 25.8 1.0
OG A:SER470 4.7 20.1 1.0
C7 A:DS9603 4.8 23.0 1.0
N3 A:DS9603 4.8 21.1 1.0
C A:TYR462 5.0 23.4 1.0
O A:DS9603 5.0 18.4 1.0

Fluorine binding site 2 out of 4 in 8hks

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Fluorine binding site 2 out of 4 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290)


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 Pamiparib(Bgb-290) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F606

b:14.4
occ:1.00
 F B:DS9606 0.0 14.4 1.0
C10 B:DS9606 1.3 14.3 1.0
C11 B:DS9606 2.3 12.8 1.0
C9 B:DS9606 2.3 15.7 1.0
O B:PHE463 3.2 19.5 1.0
CG B:GLU558 3.3 19.8 1.0
CB B:ALA464 3.3 16.6 1.0
C12 B:DS9606 3.6 13.3 1.0
C B:PHE463 3.6 16.1 1.0
CE B:LYS469 3.6 16.1 1.0
C8 B:DS9606 3.6 17.2 1.0
CD B:LYS469 3.8 13.9 1.0
CA B:ALA464 3.9 17.9 1.0
N B:ALA464 3.9 15.6 1.0
CG B:LYS469 3.9 13.7 1.0
C15 B:DS9606 4.1 13.8 1.0
O B:ASN557 4.1 18.0 1.0
CD B:GLU558 4.2 22.2 1.0
CB B:GLU558 4.3 22.3 1.0
NZ B:LYS469 4.3 15.8 1.0
CA B:GLU558 4.4 16.0 1.0
CA B:PHE463 4.5 18.0 1.0
N B:PHE463 4.6 15.3 1.0
OE1 B:GLU558 4.7 17.3 1.0
OG B:SER470 4.8 16.4 1.0
C7 B:DS9606 4.8 14.8 1.0
N3 B:DS9606 4.9 13.9 1.0
CB B:LYS469 4.9 15.7 1.0
OE2 B:GLU558 4.9 31.3 1.0
O B:DS9606 5.0 14.6 1.0

Fluorine binding site 3 out of 4 in 8hks

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Fluorine binding site 3 out of 4 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290)


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 Pamiparib(Bgb-290) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F603

b:19.8
occ:1.00
 F C:DS9603 0.0 19.8 1.0
C10 C:DS9603 1.3 14.8 1.0
C11 C:DS9603 2.3 14.7 1.0
C9 C:DS9603 2.3 15.0 1.0
CB C:ALA464 3.3 20.0 1.0
O C:PHE463 3.4 20.6 1.0
CG C:GLU558 3.4 32.4 1.0
CE C:LYS469 3.4 24.6 1.0
C12 C:DS9603 3.6 17.6 1.0
C8 C:DS9603 3.6 15.8 1.0
C C:PHE463 3.7 23.1 1.0
CD C:LYS469 3.8 22.3 1.0
CG C:LYS469 3.8 20.2 1.0
CA C:ALA464 3.9 24.8 1.0
N C:ALA464 3.9 27.4 1.0
C15 C:DS9603 4.1 13.8 1.0
NZ C:LYS469 4.1 22.9 1.0
CD C:GLU558 4.3 28.7 1.0
O C:ASN557 4.3 24.6 1.0
CA C:GLU558 4.5 24.4 1.0
CB C:GLU558 4.5 33.0 1.0
N C:PHE463 4.5 22.4 1.0
CA C:PHE463 4.6 20.8 1.0
OE2 C:GLU558 4.7 31.2 1.0
C7 C:DS9603 4.8 17.8 1.0
CB C:LYS469 4.8 21.5 1.0
OG C:SER470 4.8 17.2 1.0
N3 C:DS9603 4.9 17.1 1.0
OE1 C:GLU558 5.0 29.7 1.0
O C:DS9603 5.0 17.3 1.0

Fluorine binding site 4 out of 4 in 8hks

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Fluorine binding site 4 out of 4 in the Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib(Bgb-290)


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 Pamiparib(Bgb-290) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F604

b:25.5
occ:1.00
 F D:DS9604 0.0 25.5 1.0
C10 D:DS9604 1.3 27.0 1.0
C11 D:DS9604 2.3 24.6 1.0
C9 D:DS9604 2.3 22.9 1.0
O D:PHE463 3.1 22.8 1.0
CB D:ALA464 3.2 18.2 1.0
CG D:GLU558 3.4 27.7 1.0
CE D:LYS469 3.5 28.9 1.0
C D:PHE463 3.5 21.9 1.0
C12 D:DS9604 3.6 24.2 1.0
C8 D:DS9604 3.6 22.2 1.0
CA D:ALA464 3.7 24.6 1.0
N D:ALA464 3.7 23.5 1.0
CG D:LYS469 3.8 31.1 1.0
O D:ASN557 4.0 35.4 1.0
C15 D:DS9604 4.1 24.4 1.0
CD D:LYS469 4.2 24.2 1.0
NZ D:LYS469 4.2 34.0 1.0
CA D:GLU558 4.3 28.7 1.0
CB D:GLU558 4.3 25.8 1.0
CD D:GLU558 4.3 31.9 1.0
CA D:PHE463 4.5 19.7 1.0
N D:PHE463 4.5 20.1 1.0
OE2 D:GLU558 4.8 35.4 1.0
C7 D:DS9604 4.8 22.5 1.0
N3 D:DS9604 4.8 23.3 1.0
O D:HOH714 4.9 23.5 1.0
CB D:LYS469 4.9 33.4 1.0
C D:ASN557 5.0 31.2 1.0
O D:DS9604 5.0 23.2 1.0

Reference:

X.Y.Wang, J.Zhou, B.L.Xu. Mutated Human Adp-Ribosyltransferase 2 (PARP2) Catalytic Domain Bound to Pamiparib To Be Published.
Page generated: Fri Aug 2 20:09:26 2024

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