Zinc in PDB 5k16: Crystal Structure of Free Ubiquitin-Specific Protease 12

All present enzymatic activity of Crystal Structure of Free Ubiquitin-Specific Protease 12:
3.4.19.12;

The structure of Crystal Structure of Free Ubiquitin-Specific Protease 12, PDB code: 5k16 was solved by H.Li, A.D.D'andrea, N.Zheng, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.45 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.396, 109.636, 134.193, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 24.6

The binding sites of Zinc atom in the Crystal Structure of Free Ubiquitin-Specific Protease 12 (pdb code 5k16). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Free Ubiquitin-Specific Protease 12, PDB code: 5k16:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Free Ubiquitin-Specific Protease 12


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 Free Ubiquitin-Specific Protease 12 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:74.8 occ:1.00 SG A:CYS189 2.2 68.0 1.0 SG A:CYS186 2.3 71.6 1.0 SG A:CYS233 2.3 65.8 1.0 SG A:CYS236 2.4 83.6 1.0 CB A:CYS186 2.9 71.5 1.0 CB A:CYS236 3.1 70.4 1.0 CB A:CYS189 3.5 71.5 1.0 N A:CYS236 3.6 78.4 1.0 CB A:CYS233 3.8 76.5 1.0 N A:CYS189 3.9 77.8 1.0 CA A:CYS236 3.9 70.8 1.0 OG1 A:THR191 4.1 78.2 1.0 CA A:CYS189 4.3 72.7 1.0 CB A:GLU235 4.4 74.2 1.0 CA A:CYS186 4.4 67.0 1.0 CG A:GLN240 4.5 79.4 1.0 CB A:THR188 4.5 79.6 1.0 C A:GLU235 4.7 77.5 1.0 CB A:THR191 4.7 74.8 1.0 CG2 A:THR188 4.9 71.4 1.0 C A:THR188 4.9 78.4 1.0 C A:CYS186 5.0 71.6 1.0 C A:CYS189 5.0 78.2 1.0 CG A:GLU235 5.0 67.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Free Ubiquitin-Specific Protease 12


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Free Ubiquitin-Specific Protease 12 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:51.0 occ:1.00 SG B:CYS189 2.2 53.0 1.0 SG B:CYS233 2.3 46.2 1.0 SG B:CYS236 2.3 53.5 1.0 SG B:CYS186 2.5 54.1 1.0 CB B:CYS189 3.1 49.7 1.0 CB B:CYS186 3.2 46.1 1.0 CB B:CYS233 3.3 41.2 1.0 CB B:CYS236 3.4 53.1 1.0 N B:CYS236 3.7 59.5 1.0 N B:CYS189 4.0 54.8 1.0 CA B:CYS189 4.1 57.5 1.0 CA B:CYS236 4.1 53.5 1.0 CB B:GLU235 4.2 57.9 1.0 CG B:GLU235 4.3 62.3 1.0 C B:GLU235 4.5 58.6 1.0 CA B:CYS186 4.7 47.1 1.0 CG B:GLN240 4.7 51.6 1.0 CA B:CYS233 4.7 48.9 1.0 CA B:GLU235 4.7 57.6 1.0 C B:CYS189 4.8 52.3 1.0 O B:HOH510 4.8 42.0 1.0 N B:GLU235 4.9 53.9 1.0 CB B:THR191 4.9 60.0 1.0 CB B:GLN240 5.0 47.0 1.0 CB B:THR188 5.0 49.9 1.0

H.Li, K.S.Lim, H.Kim, T.R.Hinds, U.Jo, H.Mao, C.E.Weller, J.Sun, C.Chatterjee, A.D.D'andrea, N.Zheng. Allosteric Activation of Ubiquitin-Specific Proteases By Beta-Propeller Proteins UAF1 and WDR20. Mol.Cell V. 63 249 2016.
ISSN: ISSN 1097-2765
PubMed: 27373336
DOI: 10.1016/J.MOLCEL.2016.05.031