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Magnesium in PDB 3p0f: Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine

Enzymatic activity of Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine

All present enzymatic activity of Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine:
2.4.2.3;

Protein crystallography data

The structure of Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine, PDB code: 3p0f was solved by T.P.Roosild, S.Castronovo, A.Villoso, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.54
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 59.696, 59.696, 189.307, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 21.2

Other elements in 3p0f:

The structure of Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine also contains other interesting chemical elements:

Cobalt (Co) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine (pdb code 3p0f). 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 Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine, PDB code: 3p0f:

Magnesium binding site 1 out of 1 in 3p0f

Go back to Magnesium Binding Sites List in 3p0f
Magnesium binding site 1 out of 1 in the Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of HUPP2 in An Inactive Conformation with Bound 5- Benzylacyclouridine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg315

b:22.7
occ:1.00
 O A:HOH590 2.1 33.3 1.0
O A:HOH598 2.2 37.2 1.0
OD2 A:ASP280 2.3 22.2 1.0
OD2 A:ASP283 2.5 29.4 1.0
O A:HOH532 2.6 46.5 1.0
O A:HOH579 2.7 47.8 1.0
O A:HOH516 3.0 42.8 1.0
CG A:ASP280 3.2 17.8 1.0
CG A:ASP283 3.4 23.7 1.0
CB A:ASP280 3.7 15.8 1.0
OD1 A:ASP283 3.7 26.9 1.0
O A:HOH511 3.9 35.1 1.0
OD1 A:ASP280 4.2 15.8 1.0
O A:HOH364 4.4 45.0 1.0
CB A:ASP283 4.7 20.6 1.0

Reference:

T.P.Roosild, S.Castronovo, A.Villoso, A.Ziemba, G.Pizzorno. A Novel Structural Mechanism For Redox Regulation of Uridine Phosphorylase 2 Activity. J.Struct.Biol. V. 176 229 2011.
ISSN: ISSN 1047-8477
PubMed: 21855639
DOI: 10.1016/J.JSB.2011.08.002
Page generated: Mon Aug 11 01:42:57 2025

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