Zinc in PDB 7s68: Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break.

All present enzymatic activity of Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break.:
2.4.2.30;

The structure of Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break., PDB code: 7s68 was solved by E.Rouleau-Turcotte, J.M.Pascal, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.41 / 3.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	87.208, 93.652, 119.259, 90, 106.29, 90
R / Rfree (%)	25.1 / 29.2

The binding sites of Zinc atom in the Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break. (pdb code 7s68). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break., PDB code: 7s68:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:221.0 occ:1.00 SG A:CYS298 2.2 103.5 1.0 SG A:CYS295 2.3 178.6 1.0 SG A:CYS311 2.3 130.5 1.0 SG A:CYS321 2.3 104.3 1.0 HB2 A:CYS295 2.8 157.2 1.0 HG21 A:VAL323 2.9 148.7 1.0 CB A:CYS295 2.9 130.6 1.0 H A:CYS298 3.1 181.8 1.0 HB3 A:CYS295 3.1 157.2 1.0 HB3 A:CYS311 3.2 176.3 1.0 HB3 A:CYS298 3.2 160.4 1.0 CB A:CYS311 3.3 146.5 1.0 HB2 A:CYS311 3.4 176.3 1.0 HB3 A:CYS321 3.4 185.9 1.0 CB A:CYS298 3.4 133.2 1.0 CB A:CYS321 3.4 154.5 1.0 HB A:VAL323 3.6 137.4 1.0 CG2 A:VAL323 3.7 123.5 1.0 HB2 A:CYS321 3.7 185.9 1.0 HG23 A:VAL323 3.8 148.7 1.0 N A:CYS298 3.9 151.1 1.0 H A:GLY300 4.0 163.1 1.0 HB2 A:GLU297 4.1 203.8 1.0 HB2 A:CYS298 4.1 160.4 1.0 CB A:VAL323 4.2 114.1 1.0 CA A:CYS298 4.2 135.3 1.0 H A:GLY313 4.3 160.2 1.0 H A:GLU297 4.4 169.5 1.0 CA A:CYS295 4.4 135.3 1.0 HD11 A:LEU302 4.4 162.1 1.0 HG22 A:VAL323 4.4 148.7 1.0 H A:SER299 4.5 147.5 1.0 HA3 A:GLY313 4.6 161.7 1.0 HG11 A:VAL323 4.6 152.6 1.0 HA A:CYS295 4.6 162.9 1.0 HD12 A:LEU302 4.6 162.1 1.0 CA A:CYS311 4.7 122.5 1.0 N A:GLY300 4.8 135.5 1.0 HA3 A:GLY300 4.8 157.6 1.0 CA A:CYS321 4.8 151.7 1.0 N A:SER299 4.8 122.5 1.0 C A:CYS298 4.8 151.8 1.0 OE1 A:GLU297 5.0 134.1 1.0 CG1 A:VAL323 5.0 126.7 1.0 CB A:GLU297 5.0 169.4 1.0 H A:VAL323 5.0 152.6 1.0 HA A:CYS311 5.0 147.5 1.0 HA A:CYS298 5.0 162.8 1.0

Zinc binding site 2 out of 2 in the Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human PARP1 Domains (ZN1, ZN3, Wgr and Hd) Bound to A Dna Double Strand Break. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn402 b:155.4 occ:1.00 ND1 A:HIS53 2.0 106.7 1.0 SG A:CYS24 2.3 138.4 1.0 SG A:CYS56 2.3 140.8 1.0 SG A:CYS21 2.4 117.7 1.0 HB2 A:HIS53 2.4 183.8 1.0 HB2 A:CYS56 2.8 175.1 1.0 CG A:HIS53 2.9 140.4 1.0 H A:HIS53 2.9 162.2 1.0 H A:CYS24 3.0 165.2 1.0 CB A:HIS53 3.1 152.7 1.0 CB A:CYS56 3.1 145.5 1.0 CE1 A:HIS53 3.1 125.8 1.0 HB3 A:CYS24 3.3 174.6 1.0 HB3 A:CYS56 3.4 175.1 1.0 HE1 A:HIS53 3.4 151.5 1.0 CB A:CYS24 3.4 145.1 1.0 HB2 A:CYS21 3.5 165.2 1.0 HB3 A:LYS23 3.5 185.9 1.0 CB A:CYS21 3.5 137.3 1.0 N A:HIS53 3.6 134.7 1.0 HB3 A:CYS21 3.7 165.2 1.0 N A:CYS24 3.8 137.2 1.0 HB3 A:HIS53 3.8 183.8 1.0 CA A:HIS53 4.0 136.9 1.0 CD2 A:HIS53 4.0 146.4 1.0 NE2 A:HIS53 4.1 147.0 1.0 HB2 A:CYS24 4.2 174.6 1.0 CA A:CYS24 4.2 117.9 1.0 H A:LYS23 4.3 146.1 1.0 H A:CYS56 4.3 155.4 1.0 CB A:LYS23 4.4 154.5 1.0 HA A:TYR52 4.5 115.8 1.0 CA A:CYS56 4.5 158.4 1.0 HA A:HIS53 4.6 164.8 1.0 N A:CYS56 4.8 129.1 1.0 C A:TYR52 4.8 98.9 1.0 C A:LYS23 4.8 148.8 1.0 H A:SER25 4.8 168.4 1.0 HD2 A:HIS53 4.8 176.2 1.0 HG3 A:LYS23 4.9 206.0 1.0 HE2 A:HIS53 4.9 176.9 1.0 HG2 A:LYS23 4.9 206.0 1.0 CA A:CYS21 4.9 116.5 1.0 HA A:CYS24 4.9 142.0 1.0 N A:LYS23 5.0 121.3 1.0 HA A:CYS56 5.0 190.5 1.0 C A:HIS53 5.0 108.3 1.0 CA A:LYS23 5.0 116.7 1.0 HB3 A:TYR52 5.0 155.8 1.0

E.Rouleau-Turcotte, D.B.Krastev, S.J.Pettitt, C.J.Lord, J.M.Pascal. Captured Snapshots of PARP1 in the Active State Reveal the Mechanics of PARP1 Allostery. Mol.Cell V. 82 2939 2022.
ISSN: ISSN 1097-2765
PubMed: 35793673
DOI: 10.1016/J.MOLCEL.2022.06.011