Zinc in PDB 4q8g: Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase

All present enzymatic activity of Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase:
3.1.13.4;

The structure of Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase, PDB code: 4q8g was solved by I.B.Schaefer, E.Conti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.33 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.508, 74.032, 175.081, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 22.1

The binding sites of Zinc atom in the Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase (pdb code 4q8g). 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 the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase, PDB code: 4q8g:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn901 b:56.9 occ:1.00 HD1 A:HIS662 1.6 72.2 1.0 HB2 A:CYS716 2.0 89.3 1.0 ND1 A:HIS662 2.3 60.2 1.0 SG A:CYS713 2.3 64.9 1.0 SG A:CYS660 2.4 57.6 1.0 H A:CYS716 2.7 90.2 1.0 CB A:CYS716 2.7 74.4 1.0 HB2 A:CYS660 2.8 71.5 1.0 SG A:CYS716 2.8 0.1 1.0 HB2 A:HIS662 2.9 69.9 1.0 HB3 A:CYS713 3.0 67.8 1.0 CB A:CYS713 3.0 56.5 1.0 HB2 A:CYS713 3.1 67.8 1.0 CG A:HIS662 3.1 58.4 1.0 CB A:CYS660 3.1 59.6 1.0 CE1 A:HIS662 3.2 61.5 1.0 N A:CYS716 3.3 75.2 1.0 HE1 A:HIS662 3.4 73.8 1.0 HB3 A:CYS716 3.4 89.3 1.0 CB A:HIS662 3.5 58.3 1.0 HB A:THR715 3.5 79.0 1.0 HB3 A:CYS660 3.6 71.5 1.0 CA A:CYS716 3.6 78.4 1.0 HB3 A:HIS662 3.9 69.9 1.0 HA A:CYS716 4.1 94.1 1.0 H A:HIS662 4.2 76.7 1.0 NE2 A:HIS662 4.2 62.0 1.0 CD2 A:HIS662 4.2 57.9 1.0 H A:THR715 4.4 81.0 1.0 H A:GLY717 4.4 99.8 1.0 CB A:THR715 4.4 65.8 1.0 C A:THR715 4.4 72.8 1.0 HB3 A:LYS718 4.5 79.6 1.0 CA A:CYS660 4.5 61.6 1.0 CA A:CYS713 4.5 55.9 1.0 HE2 A:TYR663 4.5 62.0 1.0 O A:CYS660 4.5 66.9 1.0 H A:LYS718 4.5 88.9 1.0 C A:CYS660 4.6 63.9 1.0 N A:HIS662 4.7 63.9 1.0 CA A:HIS662 4.7 62.3 1.0 C A:CYS716 4.7 82.0 1.0 HA A:CYS713 4.8 67.1 1.0 CA A:THR715 4.8 68.8 1.0 N A:GLY717 4.9 83.2 1.0 N A:THR715 4.9 67.5 1.0 CE2 A:TYR663 5.0 51.6 1.0 C A:CYS713 5.0 56.8 1.0

Zinc binding site 2 out of 2 in the Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Saccharomyces Cerevisiae PAN2 Pseudoubiquitin- Hydrolase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn901 b:0.5 occ:1.00 HB2 B:CYS716 1.7 0.3 1.0 HB2 B:CYS660 1.7 0.3 1.0 SG B:CYS713 2.0 0.4 1.0 HB3 B:CYS716 2.2 0.3 1.0 CB B:CYS660 2.2 0.9 1.0 ND1 B:HIS662 2.3 86.3 1.0 CB B:CYS716 2.3 0.8 1.0 HB3 B:CYS660 2.4 0.3 1.0 SG B:CYS660 2.4 0.1 1.0 HB2 B:CYS713 2.8 0.1 1.0 CB B:CYS713 2.9 0.9 1.0 H B:CYS716 3.0 0.8 1.0 O B:ASP661 3.0 97.3 1.0 HB2 B:HIS662 3.0 0.1 1.0 HB3 B:CYS713 3.1 0.1 1.0 CE1 B:HIS662 3.2 92.8 1.0 HE1 B:HIS662 3.3 0.4 1.0 CG B:HIS662 3.3 87.8 1.0 SG B:CYS716 3.5 0.2 1.0 CA B:CYS716 3.5 0.7 1.0 N B:CYS716 3.6 0.0 1.0 CB B:HIS662 3.7 89.3 1.0 CA B:CYS660 3.7 0.1 1.0 C B:ASP661 4.0 96.2 1.0 HA B:CYS716 4.0 0.7 1.0 HA B:CYS660 4.1 0.3 1.0 HE2 B:TYR663 4.2 0.7 1.0 C B:CYS660 4.2 0.5 1.0 N B:ASP661 4.3 0.9 1.0 H B:ASP661 4.3 0.5 1.0 HB3 B:HIS662 4.3 0.1 1.0 HD2 B:TYR663 4.3 0.2 1.0 NE2 B:HIS662 4.3 95.4 1.0 HG B:CYS716 4.4 0.4 1.0 CA B:CYS713 4.4 94.7 1.0 CD2 B:HIS662 4.4 91.5 1.0 H B:CYS660 4.4 0.9 1.0 HA B:CYS713 4.5 0.7 1.0 C B:CYS716 4.6 0.3 1.0 N B:CYS660 4.6 0.6 1.0 CE2 B:TYR663 4.7 86.5 1.0 CA B:HIS662 4.7 91.6 1.0 H B:LYS718 4.7 1.0 1.0 CD2 B:TYR663 4.8 85.2 1.0 H B:GLY717 4.8 0.6 1.0 N B:HIS662 4.8 95.0 1.0 C B:THR715 4.9 0.8 1.0 CA B:ASP661 4.9 97.8 1.0

I.B.Schafer, M.Rode, F.Bonneau, S.Schussler, E.Conti. The Structure of the PAN2-PAN3 Core Complex Reveals Cross-Talk Between Deadenylase and Pseudokinase. Nat.Struct.Mol.Biol. V. 21 591 2014.
ISSN: ISSN 1545-9993
PubMed: 24880344
DOI: 10.1038/NSMB.2834