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Magnesium in PDB 2xbu: Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form)

Enzymatic activity of Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form)

All present enzymatic activity of Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form):
2.4.2.8;

Protein crystallography data

The structure of Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form), PDB code: 2xbu was solved by L.Moynie, M.F.Giraud, A.Breton, F.Boissier, B.Daignan-Fornier, A.Dautant, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.21 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.577, 77.521, 56.655, 90.00, 95.13, 90.00
R / Rfree (%) 16.7 / 20.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form) (pdb code 2xbu). 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 Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form), PDB code: 2xbu:

Magnesium binding site 1 out of 1 in 2xbu

Go back to Magnesium Binding Sites List in 2xbu
Magnesium binding site 1 out of 1 in the Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Saccharomyces Cerevisiae Hypoxanthine-Guanine Phosphoribosyltransferase in Complex with Gmp (Monoclinic Crystal Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg301

b:41.4
occ:1.00
 OD2 B:ASP110 2.5 28.5 1.0
O B:HOH2044 2.5 44.0 1.0
OE2 B:GLU111 2.5 29.6 1.0
O B:ILE36 2.6 19.7 1.0
O B:HOH2201 2.7 27.7 1.0
O B:HOH2106 2.7 31.7 1.0
N B:GLY40 3.3 18.4 1.0
CD B:GLU111 3.4 28.5 1.0
CG B:ASP110 3.5 25.4 1.0
OE1 B:GLU111 3.6 26.0 1.0
C B:ILE36 3.7 17.0 1.0
C B:GLY39 3.7 22.4 1.0
CA B:GLY39 3.7 25.0 1.0
OD1 B:ASP110 3.9 27.2 1.0
N B:GLY39 3.9 25.8 1.0
O B:HOH2029 4.0 51.4 1.0
CA B:GLY37 4.1 22.6 1.0
CA B:GLY40 4.1 18.6 1.0
C B:GLY37 4.3 22.6 1.0
N B:GLY37 4.3 19.4 1.0
O3' B:5GP1220 4.5 31.7 1.0
O A:HOH2025 4.5 46.8 1.0
CG2 B:ILE36 4.5 21.1 1.0
O B:GLY37 4.5 20.4 1.0
N B:GLU111 4.5 17.1 1.0
O B:GLY39 4.6 22.8 1.0
CB B:ILE36 4.6 20.4 1.0
CB B:ASP110 4.7 18.5 1.0
N B:GLY38 4.8 24.8 1.0
CA B:ILE36 4.8 16.0 1.0
CA B:ASP110 4.8 14.4 1.0
CG B:GLU111 4.8 20.2 1.0
C B:GLY38 5.0 28.0 1.0

Reference:

L.Moynie, M.F.Giraud, A.Breton, F.Boissier, B.Daignan-Fornier, A.Dautant. Functional Significance of Four Successive Glycine Residues in the Pyrophosphate Binding Loop of Fungal 6-Oxopurine Phosphoribosyltransferases. Protein Sci. V. 21 1185 2012.
ISSN: ISSN 0961-8368
PubMed: 22610485
DOI: 10.1002/PRO.2098
Page generated: Wed Aug 14 07:04:49 2024

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