Magnesium in PDB 2foz: Human Adp-Ribosylhydrolase 3

The structure of Human Adp-Ribosylhydrolase 3, PDB code: 2foz was solved by C.Mueller-Dieckmann, M.S.Weiss, F.Koch-Nolte, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.300, 60.400, 97.200, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 20.9

The binding sites of Magnesium atom in the Human Adp-Ribosylhydrolase 3 (pdb code 2foz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Adp-Ribosylhydrolase 3, PDB code: 2foz:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human Adp-Ribosylhydrolase 3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Adp-Ribosylhydrolase 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg348 b:11.4 occ:1.00 OD2 A:ASP300 2.0 22.3 1.0 OD2 A:ASP62 2.0 22.1 1.0 OD1 A:ASP61 2.1 21.1 1.0 O A:HOH352 2.1 11.2 1.0 OG1 A:THR60 2.1 21.3 1.0 O A:HOH350 2.2 13.6 1.0 CG A:ASP300 3.1 21.3 1.0 CB A:THR60 3.1 21.6 1.0 CG A:ASP61 3.2 23.1 1.0 CG A:ASP62 3.2 23.1 1.0 OD1 A:ASP300 3.7 21.8 1.0 MG A:MG349 3.7 11.3 1.0 OD2 A:ASP61 3.8 23.8 1.0 N A:ASP62 3.9 21.7 1.0 OD1 A:ASP18 3.9 23.3 1.0 N A:ASP61 3.9 20.5 1.0 OD1 A:ASP62 4.0 21.6 1.0 CG2 A:THR60 4.0 22.4 1.0 OE1 A:GLU25 4.0 23.7 1.0 O A:HOH373 4.0 17.6 1.0 O A:GLY99 4.2 21.7 1.0 OE2 A:GLU25 4.2 22.6 1.0 OG1 A:THR301 4.2 21.2 1.0 CB A:ASP300 4.2 21.3 1.0 CB A:ASP62 4.3 22.1 1.0 O A:HOH558 4.3 27.3 1.0 CB A:ASP61 4.4 21.1 1.0 CD A:GLU25 4.4 22.1 1.0 CA A:THR60 4.4 20.8 1.0 C A:THR60 4.4 21.3 1.0 CA A:ASP61 4.5 21.1 1.0 CA A:ASP62 4.7 21.6 1.0 C A:ASP61 4.7 22.2 1.0 CG A:ASP18 4.9 24.0 1.0

Magnesium binding site 2 out of 2 in the Human Adp-Ribosylhydrolase 3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Adp-Ribosylhydrolase 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg349 b:11.3 occ:1.00 OD1 A:ASP298 2.1 21.5 1.0 OD1 A:ASP300 2.1 21.8 1.0 O A:HOH350 2.1 13.6 1.0 OE2 A:GLU25 2.1 22.6 1.0 O A:HOH351 2.2 14.1 1.0 OG1 A:THR301 2.2 21.2 1.0 CG A:ASP300 3.0 21.3 1.0 CD A:GLU25 3.0 22.1 1.0 CG A:ASP298 3.1 22.0 1.0 CB A:THR301 3.3 22.4 1.0 OD2 A:ASP298 3.3 22.2 1.0 OD2 A:ASP300 3.3 22.3 1.0 O A:HOH389 3.7 20.0 1.0 MG A:MG348 3.7 11.4 1.0 N A:THR301 3.8 20.4 1.0 CG A:GLU25 3.8 20.2 1.0 OE1 A:GLU25 3.8 23.7 1.0 O A:HOH373 3.9 17.6 1.0 O A:HOH558 3.9 27.3 1.0 CA A:THR301 4.2 21.2 1.0 OD2 A:ASP62 4.3 22.1 1.0 O A:HOH352 4.3 11.2 1.0 OD1 A:ASP62 4.4 21.6 1.0 CB A:ASP300 4.4 21.3 1.0 CB A:ASP298 4.4 20.2 1.0 CG2 A:THR301 4.4 22.5 1.0 C A:ASP300 4.6 20.6 1.0 N A:ASP300 4.7 20.4 1.0 C A:ASP298 4.7 20.5 1.0 CA A:ASP298 4.7 20.2 1.0 CG A:ASP62 4.8 23.1 1.0 CA A:ASP300 4.8 20.8 1.0 O A:ASP298 4.8 21.3 1.0

C.Mueller-Dieckmann, S.Kernstock, M.Lisurek, J.P.Von Kries, F.Haag, M.S.Weiss, F.Koch-Nolte. The Structure of Human Adp-Ribosylhydrolase 3 (ARH3) Provides Insights Into the Reversibility of Protein Adp-Ribosylation. Proc.Natl.Acad.Sci.Usa V. 103 15026 2006.
ISSN: ISSN 0027-8424
PubMed: 17015823
DOI: 10.1073/PNAS.0606762103