Magnesium in PDB 1grv: Hypoxanthine Phosphoribosyltransferase From E. Coli

All present enzymatic activity of Hypoxanthine Phosphoribosyltransferase From E. Coli:
2.4.2.8;

The structure of Hypoxanthine Phosphoribosyltransferase From E. Coli, PDB code: 1grv was solved by L.W.Guddat, S.Vos, J.L.Martin, D.T.Keough, J.De Jersey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.0 / 2.90
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	83.900, 83.900, 169.400, 90.00, 90.00, 120.00
R / Rfree (%)	21.4 / 23.8

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

Magnesium binding site 1 out of 2 in the Hypoxanthine Phosphoribosyltransferase 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 Hypoxanthine Phosphoribosyltransferase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg490 b:22.0 occ:1.00 OE2 B:GLU103 2.0 40.1 1.0 OD1 B:ASP104 2.0 26.9 1.0 O B:HOH2024 2.1 37.9 1.0 O B:HOH2026 2.2 22.7 1.0 CD B:GLU103 2.6 39.4 1.0 CG B:GLU103 2.6 34.7 1.0 CG B:ASP104 3.1 24.8 1.0 OD2 B:ASP104 3.6 24.4 1.0 O B:HOH2025 3.6 35.9 1.0 OE1 B:GLU103 3.8 43.5 1.0 N B:ASP104 3.9 24.3 1.0 CB B:GLU103 4.0 28.9 1.0 O B:ILE105 4.0 27.0 1.0 N B:ILE105 4.2 23.9 1.0 CB B:ASP104 4.3 23.4 1.0 O B:LEU45 4.5 26.7 1.0 CA B:GLU103 4.5 26.4 1.0 CA B:ASP104 4.6 23.8 1.0 C B:GLU103 4.7 25.5 1.0 CA B:GLY48 4.7 26.4 1.0 CB B:LEU45 4.8 24.8 1.0 CG2 B:ILE105 4.9 22.1 1.0 N B:SER49 4.9 25.2 1.0 C B:GLY48 4.9 25.7 1.0 C B:ASP104 4.9 23.6 1.0 C B:ILE105 5.0 26.3 1.0

Magnesium binding site 2 out of 2 in the Hypoxanthine Phosphoribosyltransferase 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 Hypoxanthine Phosphoribosyltransferase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg491 b:29.7 occ:1.00 O A:HOH2019 2.0 30.4 1.0 OD1 A:ASP104 2.1 27.6 1.0 OE2 A:GLU103 2.1 40.5 1.0 O A:HOH2018 2.3 37.4 1.0 CD A:GLU103 2.7 39.8 1.0 CG A:GLU103 2.8 34.5 1.0 CG A:ASP104 3.1 25.4 1.0 O A:HOH2017 3.1 33.1 1.0 OD2 A:ASP104 3.5 24.8 1.0 O A:HOH2020 3.6 21.5 1.0 O A:ILE105 3.7 25.0 1.0 OE1 A:GLU103 3.8 45.6 1.0 N A:ILE105 4.1 22.9 1.0 N A:ASP104 4.1 24.1 1.0 CB A:GLU103 4.3 28.6 1.0 CB A:ASP104 4.4 23.6 1.0 CG2 A:ILE105 4.5 23.1 1.0 C A:ILE105 4.7 25.0 1.0 CA A:ASP104 4.7 23.4 1.0 CA A:GLY48 4.9 29.0 1.0 CA A:GLU103 4.9 26.1 1.0 C A:ASP104 4.9 23.2 1.0 CA A:ILE105 4.9 23.8 1.0 C A:GLU103 4.9 25.1 1.0 O A:LEU45 5.0 26.3 1.0

L.W.Guddat, S.Vos, J.L.Martin, D.T.Keough, J.De Jersey. Crystal Structures of Free, Imp-, and Gmp- Bound Escherichia Coli Hypoxanthine Phosphoribosyltransferase Protein Sci. V. 11 1626 2002.
ISSN: ISSN 0961-8368
PubMed: 12070315
DOI: 10.1110/PS.0201002