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Magnesium in PDB 1nul: Xprtase From E. Coli

Enzymatic activity of Xprtase From E. Coli

All present enzymatic activity of Xprtase From E. Coli:
2.4.2.22;

Protein crystallography data

The structure of Xprtase From E. Coli, PDB code: 1nul was solved by S.Vos, J.De Jersey, J.L.Martin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.80
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.200, 92.700, 53.200, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 23.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Xprtase From E. Coli (pdb code 1nul). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Xprtase From E. Coli, PDB code: 1nul:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1nul

Go back to Magnesium Binding Sites List in 1nul
Magnesium binding site 1 out of 2 in the Xprtase From E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Xprtase From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:44.6
occ:1.00
O A:HOH962 2.2 60.0 1.0
O A:HOH963 2.2 69.4 1.0
O A:HOH961 2.2 43.1 1.0
O A:HOH960 2.2 25.2 1.0
O A:HOH964 2.2 42.6 1.0
OD1 A:ASP89 2.3 13.0 1.0
CG A:ASP89 3.2 15.9 1.0
OD2 A:ASP89 3.5 21.0 1.0
OD1 A:ASP88 3.7 15.4 1.0
O4 A:SO4302 4.0 51.3 1.0
OD2 A:ASP88 4.1 15.4 1.0
CA A:GLY38 4.1 15.4 1.0
CG A:ASP88 4.2 14.4 1.0
O A:HOH866 4.2 51.5 1.0
O A:HOH803 4.3 45.5 1.0
O A:HOH855 4.5 59.0 1.0
N A:LEU90 4.5 14.7 1.0
O A:LEU90 4.5 18.9 1.0
O3 A:SO4302 4.5 54.6 1.0
CB A:ASP89 4.6 16.7 1.0
N A:GLY38 4.7 17.6 1.0
N A:ASP89 4.8 13.8 1.0
S A:SO4302 4.9 48.9 1.0

Magnesium binding site 2 out of 2 in 1nul

Go back to Magnesium Binding Sites List in 1nul
Magnesium binding site 2 out of 2 in the Xprtase From E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Xprtase From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:59.1
occ:1.00
O B:HOH959 2.2 64.3 1.0
O B:HOH955 2.2 57.6 1.0
O B:HOH956 2.2 42.1 1.0
OD1 B:ASP89 2.4 18.0 1.0
O B:HOH957 2.4 27.3 1.0
O B:HOH958 2.4 53.9 1.0
CG B:ASP89 3.3 20.6 1.0
OD2 B:ASP89 3.6 21.5 1.0
OD1 B:ASP88 3.8 15.6 1.0
CA B:GLY38 4.0 16.5 1.0
O B:HOH856 4.1 48.5 1.0
OD2 B:ASP88 4.3 18.1 1.0
O1 B:SO4301 4.4 59.4 1.0
CG B:ASP88 4.4 17.5 1.0
N B:GLY38 4.5 17.0 1.0
O B:HOH706 4.6 40.7 1.0
N B:LEU90 4.6 17.0 1.0
CB B:ASP89 4.7 16.2 1.0
O B:HOH762 4.7 46.3 1.0
O B:LEU90 4.7 22.7 1.0
N B:ASP89 4.9 13.6 1.0
O2 B:SO4301 4.9 63.0 1.0
C B:GLY38 4.9 16.9 1.0

Reference:

S.Vos, J.De Jersey, J.L.Martin. Crystal Structure of Escherichia Coli Xanthine Phosphoribosyltransferase. Biochemistry V. 36 4125 1997.
ISSN: ISSN 0006-2960
PubMed: 9100006
DOI: 10.1021/BI962640D
Page generated: Tue Aug 13 10:23:18 2024

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