Magnesium in PDB 3shq: Crystal Structure of UBLCP1

All present enzymatic activity of Crystal Structure of UBLCP1:
3.1.3.16;

The structure of Crystal Structure of UBLCP1, PDB code: 3shq was solved by J.Xiao, J.L.Engel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.00 / 1.96
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	101.813, 101.813, 90.936, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 20.7

The binding sites of Magnesium atom in the Crystal Structure of UBLCP1 (pdb code 3shq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of UBLCP1, PDB code: 3shq:

Magnesium binding site 1 out of 1 in the Crystal Structure of UBLCP1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of UBLCP1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg321 b:25.2 occ:1.00 O A:HOH322 2.0 21.4 1.0 OD1 A:ASP148 2.1 25.2 1.0 O A:ASP148 2.1 20.6 1.0 O A:HOH344 2.1 25.8 1.0 OD2 A:ASP146 2.1 20.9 1.0 OD2 A:ASP255 2.2 24.2 1.0 CG A:ASP146 3.0 24.0 1.0 CG A:ASP148 3.1 29.3 1.0 C A:ASP148 3.2 18.9 1.0 CG A:ASP255 3.2 27.8 1.0 OD1 A:ASP146 3.3 21.6 1.0 OD1 A:ASP255 3.6 25.0 1.0 CA A:ASP148 3.7 21.8 1.0 N A:ASP148 3.8 20.5 1.0 CB A:ASP148 3.9 26.9 1.0 OD2 A:ASP148 3.9 29.6 1.0 OD1 A:ASP254 4.0 23.6 1.0 OG1 A:THR150 4.1 24.5 1.0 O A:HOH338 4.2 23.9 1.0 N A:TYR149 4.4 23.0 1.0 CB A:ASP146 4.4 17.2 1.0 CB A:ASP255 4.5 21.3 1.0 CG1 A:ILE256 4.5 27.9 1.0 O A:HOH352 4.5 29.1 1.0 N A:ASP255 4.5 20.6 1.0 CB A:TYR149 4.5 22.9 1.0 O A:HOH358 4.6 27.1 1.0 O A:HOH445 4.6 31.4 1.0 C A:ILE147 4.6 25.1 1.0 O A:GLU96 4.7 26.0 1.0 N A:THR150 4.7 23.3 1.0 CA A:TYR149 4.8 25.1 1.0 CG A:ASP254 4.9 22.3 1.0 C A:TYR149 5.0 29.0 1.0 CB A:THR150 5.0 24.4 1.0

X.Guo, J.L.Engel, J.Xiao, V.S.Tagliabracci, X.Wang, L.Huang, J.E.Dixon. UBLCP1 Is A 26S Proteasome Phosphatase That Regulates Nuclear Proteasome Activity. Proc.Natl.Acad.Sci.Usa V. 108 18649 2011.
ISSN: ISSN 0027-8424
PubMed: 21949367
DOI: 10.1073/PNAS.1113170108