Magnesium in PDB 2fp0: Human Adp-Ribosylhydrolase 3

The structure of Human Adp-Ribosylhydrolase 3, PDB code: 2fp0 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)	30.00 / 2.05
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.330, 60.630, 102.880, 90.00, 96.43, 90.00
R / Rfree (%)	18.8 / 23.1

The binding sites of Magnesium atom in the Human Adp-Ribosylhydrolase 3 (pdb code 2fp0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Human Adp-Ribosylhydrolase 3, PDB code: 2fp0:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 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:Mg401 b:19.5 occ:1.00 OD1 A:ASP61 2.2 50.0 1.0 OD2 A:ASP300 2.2 52.6 1.0 O A:HOH405 2.3 41.5 1.0 OD2 A:ASP62 2.3 43.5 1.0 O A:HOH406 2.4 28.5 1.0 OG1 A:THR60 2.5 46.5 1.0 O A:HOH407 2.5 37.3 1.0 O A:HOH403 2.8 32.3 1.0 CG A:ASP300 3.2 53.0 1.0 CG A:ASP61 3.4 53.7 1.0 CG A:ASP62 3.5 47.0 1.0 CB A:THR60 3.5 40.1 1.0 MG A:MG402 3.8 29.0 1.0 CB A:ASP300 3.9 46.2 1.0 OD1 A:ASP300 4.0 48.6 1.0 OD2 A:ASP61 4.0 47.0 1.0 OD1 A:ASP62 4.1 47.0 1.0 OD1 A:ASP18 4.2 45.2 1.0 CG2 A:THR60 4.2 43.0 1.0 N A:ASP61 4.3 47.3 1.0 OE2 A:GLU25 4.3 61.4 1.0 N A:ASP62 4.4 44.5 1.0 OG A:SER22 4.4 43.8 1.0 O A:GLY99 4.6 43.6 1.0 OG1 A:THR301 4.6 44.5 1.0 CB A:ASP62 4.7 42.8 1.0 CB A:ASP61 4.7 49.5 1.0 CA A:THR60 4.8 43.2 1.0 CA A:ASP61 4.9 45.8 1.0 C A:THR60 4.9 44.7 1.0 CD A:GLU25 4.9 53.0 1.0

Magnesium binding site 2 out of 4 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:Mg402 b:29.0 occ:1.00 OD1 A:ASP298 2.3 66.4 1.0 O A:HOH407 2.4 37.3 1.0 O A:HOH404 2.4 64.4 1.0 OD1 A:ASP300 2.5 48.6 1.0 OD2 A:ASP300 2.5 52.6 1.0 OG1 A:THR301 2.6 44.5 1.0 O A:HOH403 2.7 32.3 1.0 CG A:ASP300 2.8 53.0 1.0 CG A:ASP298 3.2 50.6 1.0 OD2 A:ASP298 3.3 63.0 1.0 CB A:THR301 3.6 45.5 1.0 MG A:MG401 3.8 19.5 1.0 N A:THR301 4.0 47.4 1.0 OE2 A:GLU25 4.2 61.4 1.0 CB A:ASP300 4.3 46.2 1.0 OD1 A:ASP62 4.3 47.0 1.0 CA A:THR301 4.4 45.9 1.0 OD2 A:ASP62 4.5 43.5 1.0 CB A:ASP298 4.6 43.9 1.0 CG2 A:THR301 4.8 47.1 1.0 C A:ASP300 4.8 47.4 1.0 O A:HOH406 4.8 28.5 1.0 CG A:ASP62 4.9 47.0 1.0 CA A:ASP300 4.9 46.0 1.0 OD1 A:ASN135 5.0 46.8 1.0

Magnesium binding site 3 out of 4 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 3 of Human Adp-Ribosylhydrolase 3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:27.0 occ:1.00 OD1 B:ASP61 2.1 50.2 1.0 OD2 B:ASP300 2.1 52.5 1.0 OD2 B:ASP62 2.1 46.6 1.0 O B:HOH529 2.2 50.9 1.0 O B:HOH531 2.4 43.5 1.0 OG1 B:THR60 2.4 42.3 1.0 O B:HOH528 2.7 64.5 1.0 O B:HOH527 2.8 44.1 1.0 CG B:ASP300 3.3 50.8 1.0 CG B:ASP61 3.3 51.5 1.0 CG B:ASP62 3.4 42.9 1.0 CB B:THR60 3.4 44.9 1.0 OD2 B:ASP61 3.8 46.2 1.0 MG B:MG502 3.9 37.0 1.0 OD1 B:ASP62 4.0 48.5 1.0 CB B:ASP300 4.0 45.2 1.0 CG2 B:THR60 4.1 47.2 1.0 N B:ASP61 4.1 46.0 1.0 OD1 B:ASP300 4.2 51.1 1.0 N B:ASP62 4.3 44.8 1.0 OE2 B:GLU25 4.3 56.9 1.0 OD1 B:ASP18 4.3 45.4 1.0 O B:GLY99 4.5 43.0 1.0 OG B:SER22 4.5 42.5 1.0 CB B:ASP62 4.5 44.2 1.0 CB B:ASP61 4.6 47.9 1.0 OG1 B:THR301 4.6 44.1 1.0 O B:HOH544 4.7 45.0 1.0 CA B:THR60 4.7 45.4 1.0 CD B:GLU25 4.8 49.9 1.0 CA B:ASP61 4.8 46.1 1.0 C B:THR60 4.8 45.6 1.0 CA B:ASP62 5.0 44.2 1.0

Magnesium binding site 4 out of 4 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 4 of Human Adp-Ribosylhydrolase 3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:37.0 occ:1.00 OD1 B:ASP298 2.3 55.3 1.0 O B:HOH528 2.4 64.5 1.0 OG1 B:THR301 2.5 44.1 1.0 O B:HOH530 2.5 50.5 1.0 OD1 B:ASP300 2.6 51.1 1.0 O B:HOH527 2.6 44.1 1.0 OD2 B:ASP300 2.6 52.5 1.0 CG B:ASP300 2.9 50.8 1.0 CG B:ASP298 3.1 46.7 1.0 OD2 B:ASP298 3.1 54.9 1.0 CB B:THR301 3.6 44.9 1.0 MG B:MG501 3.9 27.0 1.0 OE2 B:GLU25 4.1 56.9 1.0 N B:THR301 4.1 44.7 1.0 OD1 B:ASP62 4.3 48.5 1.0 CB B:ASP300 4.4 45.2 1.0 OD2 B:ASP62 4.4 46.6 1.0 CA B:THR301 4.5 44.8 1.0 CB B:ASP298 4.5 45.5 1.0 CG2 B:THR301 4.7 49.6 1.0 CG B:ASP62 4.8 42.9 1.0 O B:HOH529 4.8 50.9 1.0 O B:HOH531 4.9 43.5 1.0 CD B:GLU25 4.9 49.9 1.0 C B:ASP300 4.9 44.8 1.0 OD1 B:ASN135 5.0 44.6 1.0 O B:ASP298 5.0 45.3 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