Magnesium in PDB 2xrf: Crystal Structure of Human Uridine Phosphorylase 2

All present enzymatic activity of Crystal Structure of Human Uridine Phosphorylase 2:
2.4.2.3;

The structure of Crystal Structure of Human Uridine Phosphorylase 2, PDB code: 2xrf was solved by M.Welin, M.Moche, C.H.Arrowsmith, H.Berglund, C.Bountra, R.Collins, A.M.Edwards, S.Flodin, A.Flores, S.Graslund, M.Hammarstrom, I.Johansson, T.Karlberg, S.Kol, T.Kotenyova, E.Kouznetsova, T.Nyman, C.Persson, H.Schuler, P.Schutz, M.I.Siponen, A.G.Thorsell, L.Tresaugues, S.Van Der Berg, E.Wahlberg, J.Weigelt, P.Nordlund, Structural Genomics Consortium, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.67 / 2.30
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.280, 95.280, 186.280, 90.00, 90.00, 120.00
R / Rfree (%)	16.77 / 20.65

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

Magnesium binding site 1 out of 3 in the Crystal Structure of Human Uridine Phosphorylase 2


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 Uridine Phosphorylase 2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg400 b:22.8 occ:1.00 O C:CYS95 2.3 22.5 1.0 O C:TYR101 2.3 21.8 1.0 OD2 C:ASP93 2.4 22.4 1.0 O C:THR98 2.4 20.3 1.0 O C:HOH2034 2.7 34.4 1.0 C C:CYS95 3.3 23.9 1.0 CG C:ASP93 3.3 21.5 1.0 C C:TYR101 3.4 23.1 1.0 SG C:CYS102 3.5 26.9 0.5 OD1 C:ASP93 3.6 20.8 1.0 C C:THR98 3.6 21.2 1.0 CA C:CYS102 3.7 19.3 0.5 CA C:CYS102 3.7 21.1 0.5 CB C:CYS95 3.8 18.4 1.0 N C:CYS102 3.9 19.3 0.5 N C:CYS102 3.9 20.5 0.5 O C:HOH2032 4.0 42.8 1.0 CA C:CYS95 4.2 18.9 1.0 N C:ALA96 4.2 21.5 1.0 CB C:CYS102 4.2 22.5 0.5 CB C:CYS102 4.2 20.1 0.5 CA C:ALA96 4.3 22.0 1.0 CG2 C:THR98 4.4 20.4 1.0 CA C:ASP99 4.4 18.6 1.0 N C:ASP99 4.5 18.3 1.0 N C:THR98 4.5 19.4 1.0 CA C:TYR101 4.6 18.8 1.0 CA C:THR98 4.6 18.3 1.0 N C:TYR101 4.6 18.3 1.0 C C:ALA96 4.7 25.7 1.0 CB C:ASP93 4.7 19.6 1.0 O C:ALA96 4.8 26.1 1.0 N C:CYS95 4.9 19.2 1.0 C C:CYS102 4.9 21.9 0.5 C C:ASP99 4.9 21.7 1.0 C C:CYS102 4.9 22.7 0.5

Magnesium binding site 2 out of 3 in the Crystal Structure of Human Uridine Phosphorylase 2


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 Uridine Phosphorylase 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg400 b:29.8 occ:1.00 O A:THR98 2.2 25.6 1.0 O A:CYS95 2.3 27.8 1.0 O A:TYR101 2.4 23.6 1.0 OD2 A:ASP93 2.5 30.7 1.0 C A:CYS95 3.1 26.8 1.0 C A:THR98 3.4 26.6 1.0 CG A:ASP93 3.4 26.1 1.0 C A:TYR101 3.5 24.3 1.0 SG A:CYS102 3.7 29.2 0.5 OD1 A:ASP93 3.7 23.1 1.0 N A:ALA96 3.8 24.4 1.0 CA A:ALA96 3.9 24.2 1.0 CA A:CYS102 3.9 19.1 0.5 CA A:CYS102 3.9 22.9 0.5 CB A:CYS95 3.9 21.3 1.0 N A:CYS102 4.1 19.5 0.5 N A:CYS102 4.1 22.1 0.5 N A:THR98 4.1 23.9 1.0 CA A:CYS95 4.1 20.9 1.0 O A:HOH2035 4.1 28.3 1.0 C A:ALA96 4.2 27.7 1.0 CG2 A:THR98 4.2 24.5 1.0 CB A:CYS102 4.3 19.3 0.5 CA A:THR98 4.3 22.6 1.0 O A:ALA96 4.3 26.5 1.0 CB A:CYS102 4.4 24.4 0.5 N A:ASP99 4.4 22.9 1.0 CA A:ASP99 4.5 23.1 1.0 N A:TYR101 4.7 18.0 1.0 CA A:TYR101 4.7 18.3 1.0 CB A:ASP93 4.8 23.7 1.0 N A:GLY97 4.8 24.4 1.0 CB A:THR98 4.8 28.7 1.0 N A:CYS95 4.9 20.4 1.0 C A:ASP99 5.0 26.6 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Human Uridine Phosphorylase 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Human Uridine Phosphorylase 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg400 b:21.8 occ:1.00 O B:CYS95 2.1 18.8 1.0 O B:THR98 2.3 22.8 1.0 OD2 B:ASP93 2.3 22.0 1.0 O B:TYR101 2.4 20.1 1.0 O B:HOH2034 2.8 40.5 1.0 C B:CYS95 3.0 21.0 1.0 CG B:ASP93 3.3 19.3 1.0 C B:TYR101 3.5 20.8 1.0 SG B:CYS102 3.5 22.7 0.5 C B:THR98 3.5 24.1 1.0 OD1 B:ASP93 3.6 16.4 1.0 CB B:CYS95 3.7 18.6 1.0 CA B:CYS102 3.7 19.0 0.5 CA B:CYS102 3.7 20.1 0.5 N B:ALA96 3.8 18.9 1.0 CA B:CYS95 3.9 18.5 1.0 N B:CYS102 4.0 19.3 1.0 O B:HOH2031 4.0 33.7 1.0 CA B:ALA96 4.0 19.0 1.0 CB B:CYS102 4.2 19.1 0.5 CB B:CYS102 4.2 21.1 0.5 N B:THR98 4.2 21.8 1.0 CG2 B:THR98 4.3 22.8 1.0 CA B:THR98 4.4 20.6 1.0 C B:ALA96 4.4 24.0 1.0 N B:ASP99 4.5 21.0 1.0 CA B:ASP99 4.5 20.5 1.0 CB B:ASP93 4.7 19.2 1.0 O B:HOH2035 4.7 26.1 1.0 N B:CYS95 4.7 18.6 1.0 CA B:TYR101 4.7 16.8 1.0 N B:TYR101 4.8 17.1 1.0 O B:ALA96 4.8 24.1 1.0 N B:GLY97 4.9 20.9 1.0 C B:CYS102 4.9 23.2 1.0 O B:HOH2033 4.9 43.9 1.0 CB B:THR98 4.9 26.1 1.0

M.Welin, M.Moche, C.H.Arrowsmith, H.Berglund, C.Bountra, R.Collins, A.M.Edwards, S.Flodin, A.Flores, S.Graslund, M.Hammarstrom, I.Johansson, T.Karlberg, S.Kol, T.Kotenyova, E.Kouznetsova, T.Nyman, C.Persson, H.Schuler, P.Schutz, M.I.Siponen, A.G.Thorsell, L.Tresaugues, S.Van Der Berg, E.Wahlberg, J.Weigelt, P.Nordlund. Crystal Structure of Human Uridine Phosphorylase 2 To Be Published.