Magnesium in PDB 1jls: Structure of the Uracil Phosphoribosyltransferase Uracil/Cpr 2 Mutant C128V

All present enzymatic activity of Structure of the Uracil Phosphoribosyltransferase Uracil/Cpr 2 Mutant C128V:
2.4.2.9;

The structure of Structure of the Uracil Phosphoribosyltransferase Uracil/Cpr 2 Mutant C128V, PDB code: 1jls was solved by M.A.Schumacher, C.J.Bashor, K.Otsu, S.Zu, R.Parry, B.Ullman, R.G.Brennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.03 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	71.400, 111.400, 71.900, 90.00, 97.70, 90.00
R / Rfree (%)	23.2 / 28.8

The binding sites of Magnesium atom in the Structure of the Uracil Phosphoribosyltransferase Uracil/Cpr 2 Mutant C128V (pdb code 1jls). 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 the Uracil Phosphoribosyltransferase Uracil/Cpr 2 Mutant C128V, PDB code: 1jls:

Magnesium binding site 1 out of 1 in the Structure of the Uracil Phosphoribosyltransferase Uracil/Cpr 2 Mutant C128V


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Uracil Phosphoribosyltransferase Uracil/Cpr 2 Mutant C128V within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg3756 b:45.7 occ:1.00 O1B B:PRP301 1.8 46.4 1.0 O2B B:PRP301 2.4 50.1 1.0 PB B:PRP301 2.4 61.3 1.0 O3A B:PRP301 3.1 52.4 1.0 N B:ALA113 3.2 49.3 1.0 CB B:ALA113 3.2 46.7 1.0 O1 B:PRP301 3.4 44.2 1.0 O B:HOH830 3.4 76.4 1.0 O B:VAL111 3.5 55.0 1.0 O2 B:PRP301 3.5 38.5 1.0 CB B:ARG112 3.7 50.7 1.0 CA B:ALA113 3.8 48.9 1.0 O3B B:PRP301 3.8 50.2 1.0 PA B:PRP301 3.9 59.0 1.0 O3 B:PRP301 4.2 40.5 1.0 C B:ARG112 4.3 50.0 1.0 CA B:ARG112 4.5 51.1 1.0 C B:VAL111 4.5 52.5 1.0 C2 B:PRP301 4.5 27.0 1.0 C1 B:PRP301 4.5 31.4 1.0 O1A B:PRP301 4.8 50.5 1.0 CG B:ARG112 4.8 51.1 1.0 NE B:ARG112 4.9 65.3 1.0 O B:HOH706 4.9 73.9 1.0 O2A B:PRP301 4.9 45.5 1.0 N B:ARG112 4.9 56.0 1.0 C3 B:PRP301 5.0 30.7 1.0

M.A.Schumacher, C.J.Bashor, M.H.Song, K.Otsu, S.Zhu, R.J.Parry, B.Ullman, R.G.Brennan. The Structural Mechanism of Gtp Stabilized Oligomerization and Catalytic Activation of the Toxoplasma Gondii Uracil Phosphoribosyltransferase. Proc.Natl.Acad.Sci.Usa V. 99 78 2002.
ISSN: ISSN 0027-8424
PubMed: 11773618
DOI: 10.1073/PNAS.012399599