Magnesium in PDB 3eue: Crystal Structure of Ligand-Free Human Uridine Phosphorylase 1 (HUPP1)

All present enzymatic activity of Crystal Structure of Ligand-Free Human Uridine Phosphorylase 1 (HUPP1):
2.4.2.3;

The structure of Crystal Structure of Ligand-Free Human Uridine Phosphorylase 1 (HUPP1), PDB code: 3eue was solved by T.P.Roosild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	F 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	253.777, 253.777, 253.777, 90.00, 90.00, 90.00
R / Rfree (%)	20.4 / 22.1

The binding sites of Magnesium atom in the Crystal Structure of Ligand-Free Human Uridine Phosphorylase 1 (HUPP1) (pdb code 3eue). 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 Ligand-Free Human Uridine Phosphorylase 1 (HUPP1), PDB code: 3eue:

Magnesium binding site 1 out of 1 in the Crystal Structure of Ligand-Free Human Uridine Phosphorylase 1 (HUPP1)


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 Ligand-Free Human Uridine Phosphorylase 1 (HUPP1) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg311 b:35.5 occ:1.00 OD1 A:ASP212 2.0 63.6 1.0 CG A:ASP212 3.2 56.1 1.0 N A:PHE213 3.3 49.4 1.0 N A:TYR214 3.4 45.5 1.0 CD1 A:TYR214 3.8 39.1 1.0 CB A:PHE213 3.9 46.1 1.0 CA A:PHE213 4.0 47.5 1.0 OD2 A:ASP212 4.0 58.0 1.0 C A:PHE213 4.2 47.4 1.0 CB A:TYR214 4.2 43.2 1.0 C A:ASP212 4.2 51.8 1.0 CB A:ASP212 4.3 53.0 1.0 CA A:ASP212 4.3 52.7 1.0 CA A:TYR214 4.4 44.8 1.0 CG A:TYR214 4.5 42.0 1.0 O A:HOH383 4.6 58.6 1.0 CE1 A:TYR214 4.8 38.8 1.0

T.P.Roosild, S.Castronovo, M.Fabbiani, G.Pizzorno. Implications of the Structure of Human Uridine Phosphorylase 1 on the Development of Novel Inhibitors For Improving the Therapeutic Window of Fluoropyrimidine Chemotherapy. Bmc Struct.Biol. V. 9 14 2009.
ISSN: ESSN 1472-6807
PubMed: 19291308
DOI: 10.1186/1472-6807-9-14