Magnesium in PDB 5ao0: Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp

The structure of Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp, PDB code: 5ao0 was solved by D.Schwefel, I.A.Taylor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.423 / 3.73
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	163.173, 163.173, 260.716, 90.00, 90.00, 120.00
R / Rfree (%)	21.88 / 26.77

The structure of Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp (pdb code 5ao0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp, PDB code: 5ao0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp


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 Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg3001 b:93.5 occ:1.00 O1B A:DG32002 2.6 1.0 1.0 O2B A:DG32002 2.9 0.7 1.0 PB A:DG32002 3.3 0.1 1.0 O A:HOH4002 3.8 65.5 1.0 C5' A:DG32002 4.2 65.0 1.0 O3A A:DG32002 4.3 65.6 1.0 O1G A:DG32002 4.5 0.1 1.0 O3B A:DG32002 4.5 74.4 1.0 C3' A:DG32002 4.5 49.4 1.0 O5' A:DG32002 4.5 70.1 1.0 O2G A:DG32002 4.6 0.8 1.0 C4' A:DG32002 4.7 56.0 1.0 PG A:DG32002 4.8 0.3 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human SAMHD1 (Amino Acid Residues 41-583) Bound to Ddgtp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg3001 b:65.1 occ:1.00 O2G B:DG32002 2.1 0.9 1.0 PG B:DG32002 3.1 0.2 1.0 O2B B:DG32002 3.2 1.0 1.0 O3G B:DG32002 3.2 0.8 1.0 O3B B:DG32002 3.8 0.3 1.0 PB B:DG32002 4.0 0.8 1.0 C5' B:DG32002 4.1 72.9 1.0 O1G B:DG32002 4.4 0.5 1.0 O3A B:DG32002 4.5 0.5 1.0 O B:HOH4001 4.8 89.7 1.0 C4' B:DG32002 4.9 70.3 1.0 CE B:LYS116 5.0 0.1 1.0

L.H.Arnold, H.C.Groom, S.Kunzelmann, D.Schwefel, S.J.Caswell, P.Ordonez, M.C.Mann, S.Rueschenbaum, D.C.Goldstone, S.Pennell, S.A.Howell, J.P.Stoye, M.Webb, I.A.Taylor, K.N.Bishop. Phospho-Dependent Regulation of SAMHD1 Oligomerisation Couples Catalysis and Restriction. Plos Pathog. V. 11 05194 2015.
ISSN: ISSN 1553-7366
PubMed: 26431200
DOI: 10.1371/JOURNAL.PPAT.1005194