Magnesium in PDB 6g2a: Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm

All present enzymatic activity of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm:
3.2.2.19;

The structure of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm, PDB code: 6g2a was solved by A.Ariza, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	78.09 / 1.80
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	98.526, 42.940, 89.231, 90.00, 118.93, 90.00
R / Rfree (%)	18.1 / 22

The structure of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm (pdb code 6g2a). 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 [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm, PDB code: 6g2a:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:15.2 occ:1.00 OD2 A:ASP304 2.0 15.2 1.0 OD1 A:ASP56 2.0 14.3 1.0 OD1 A:ASP55 2.1 16.0 1.0 O A:HOH545 2.1 14.8 1.0 O2N A:A3R401 2.1 16.2 1.0 OG A:SER54 2.1 13.7 1.0 CG A:ASP55 3.1 15.9 1.0 CG A:ASP304 3.2 16.5 1.0 CB A:SER54 3.2 14.5 1.0 CG A:ASP56 3.2 14.5 1.0 C2N A:A3R401 3.4 17.6 1.0 OD2 A:ASP55 3.6 15.8 1.0 N A:ASP56 3.8 13.2 1.0 CB A:ASP304 3.8 16.1 1.0 O A:HOH622 3.9 25.5 1.0 N A:ASP55 4.0 13.6 1.0 OD2 A:ASP56 4.0 14.8 1.0 OD1 A:ASP15 4.0 13.5 1.0 OD1 A:ASP304 4.1 17.9 1.0 C1N A:A3R401 4.2 18.5 1.0 O A:ARG97 4.2 15.1 1.0 CB A:ASP56 4.3 13.7 1.0 CA A:SER54 4.4 14.3 1.0 CB A:ASP55 4.4 14.8 1.0 C A:SER54 4.4 13.9 1.0 O A:ALA98 4.5 16.7 1.0 CA A:ASP55 4.5 14.1 1.0 OG A:SER305 4.6 15.5 1.0 C3N A:A3R401 4.6 18.0 1.0 CA A:ASP56 4.6 13.5 1.0 C A:ASP55 4.6 13.7 1.0 N4N A:A3R401 4.9 18.4 1.0 CD1 A:TYR19 5.0 16.2 1.0

Magnesium binding site 2 out of 2 in the Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human [Protein Adp-Ribosylargenine] Hydrolase ARH1 in Complex with Adp-Hpm within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:27.5 occ:1.00 O A:HOH512 2.1 26.4 1.0 O A:HOH575 2.1 25.3 1.0 O A:HOH638 2.1 28.3 1.0 O A:HOH628 2.1 29.1 1.0 O A:HOH526 2.1 28.2 1.0 O A:HOH502 2.2 26.6 1.0 OD2 A:ASP95 4.0 22.8 1.0 OD1 A:ASP95 4.0 23.0 1.0 CG A:ASP95 4.3 21.9 1.0 O A:GLU92 4.6 20.6 1.0

J.G.M.Rack, A.Ariza, B.S.Drown, C.Henfrey, E.Bartlett, T.Shirai, P.J.Hergenrother, I.Ahel. (Adp-Ribosyl)Hydrolases: Structural Basis For Differential Substrate Recognition and Inhibition. Cell Chem Biol V. 25 1533 2018.
ISSN: ESSN 2451-9448
PubMed: 30472116
DOI: 10.1016/J.CHEMBIOL.2018.11.001