Zinc in PDB 5xve: Crystal Structure of Human USP2 C276S Mutant in Complex with Ubiquitin

All present enzymatic activity of Crystal Structure of Human USP2 C276S Mutant in Complex with Ubiquitin:
3.4.19.12;

The structure of Crystal Structure of Human USP2 C276S Mutant in Complex with Ubiquitin, PDB code: 5xve was solved by C.Y.Chou, H.C.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.24
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.473, 54.011, 74.753, 90.00, 107.79, 90.00
R / Rfree (%)	14.7 / 16.4

The binding sites of Zinc atom in the Crystal Structure of Human USP2 C276S Mutant in Complex with Ubiquitin (pdb code 5xve). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human USP2 C276S Mutant in Complex with Ubiquitin, PDB code: 5xve:

Zinc binding site 1 out of 1 in the Crystal Structure of Human USP2 C276S Mutant in Complex with Ubiquitin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human USP2 C276S Mutant in Complex with Ubiquitin within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:13.7 occ:1.00 SG A:CYS476 2.3 16.7 1.0 SG A:CYS428 2.3 13.0 1.0 SG A:CYS425 2.3 12.3 1.0 SG A:CYS479 2.3 16.8 1.0 CB A:CYS425 3.1 11.4 1.0 CB A:CYS428 3.2 12.4 1.0 CB A:CYS476 3.3 16.6 1.0 CB A:CYS479 3.5 17.5 1.0 N A:CYS428 3.7 12.5 1.0 N A:CYS479 3.8 19.1 1.0 CA A:CYS428 4.0 12.3 1.0 CA A:CYS479 4.3 20.0 1.0 CB A:ARG478 4.4 21.2 1.0 CG A:LYS483 4.5 14.7 1.0 CA A:CYS425 4.6 11.2 1.0 CB A:ASP427 4.6 16.5 1.0 CA A:CYS476 4.7 17.7 1.0 C A:ARG478 4.8 20.7 1.0 C A:ASP427 4.8 14.1 1.0 C A:CYS428 4.8 11.6 1.0 O A:HOH1030 4.9 27.9 1.0 N A:GLY429 5.0 11.5 1.0

S.J.Chuang, S.C.Cheng, H.C.Tang, C.Y.Sun, C.Y.Chou. 6-Thioguanine Is A Noncompetitive and Slow Binding Inhibitor of Human Deubiquitinating Protease USP2 Sci Rep V. 8 3102 2018.
ISSN: ESSN 2045-2322
PubMed: 29449607
DOI: 10.1038/S41598-018-21476-W