Zinc in PDB 5k1c: Crystal Structure of the UAF1/WDR20/USP12 Complex

All present enzymatic activity of Crystal Structure of the UAF1/WDR20/USP12 Complex:
3.4.19.12;

The structure of Crystal Structure of the UAF1/WDR20/USP12 Complex, PDB code: 5k1c 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)	50.01 / 3.00
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	217.903, 217.903, 223.819, 90.00, 90.00, 120.00
R / Rfree (%)	23 / 27.1

The binding sites of Zinc atom in the Crystal Structure of the UAF1/WDR20/USP12 Complex (pdb code 5k1c). 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 the UAF1/WDR20/USP12 Complex, PDB code: 5k1c:

Zinc binding site 1 out of 1 in the Crystal Structure of the UAF1/WDR20/USP12 Complex


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 the UAF1/WDR20/USP12 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:60.0 occ:1.00 SG A:CYS189 1.3 63.7 1.0 SG A:CYS186 1.3 62.2 1.0 SG A:CYS233 1.8 77.1 1.0 CB A:CYS186 2.2 63.8 1.0 CB A:CYS189 2.4 53.4 1.0 CB A:CYS233 2.7 67.3 1.0 SG A:CYS236 2.7 58.3 1.0 CB A:CYS236 3.5 59.2 1.0 CA A:CYS189 3.5 63.0 1.0 N A:CYS189 3.5 69.8 1.0 CA A:CYS186 3.6 70.8 1.0 N A:CYS236 3.9 71.8 1.0 CA A:CYS233 4.1 68.2 1.0 CG2 A:THR191 4.1 93.3 1.0 CA A:CYS236 4.3 67.6 1.0 N A:CYS186 4.4 71.5 1.0 C A:CYS186 4.7 80.2 1.0 C A:CYS189 4.7 70.2 1.0 C A:THR188 4.8 60.3 1.0 CB A:GLU235 4.8 85.8 1.0 C A:CYS233 4.9 76.6 1.0 N A:GLU190 4.9 67.7 1.0 C A:GLU235 5.0 67.3 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