Magnesium in PDB 2bc9: Crystal-Structure of the N-Terminal Large Gtpase Domain of Human Guanylate Binding Protein 1 (HGBP1) in Complex with Non-Hydrolysable Gtp Analogue Gppnhp

The structure of Crystal-Structure of the N-Terminal Large Gtpase Domain of Human Guanylate Binding Protein 1 (HGBP1) in Complex with Non-Hydrolysable Gtp Analogue Gppnhp, PDB code: 2bc9 was solved by A.Ghosh, G.J.K.Praefcke, L.Renault, A.Wittinghofer, C.Herrmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.80
Space group	I 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.884, 101.104, 149.261, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 26.9

The binding sites of Magnesium atom in the Crystal-Structure of the N-Terminal Large Gtpase Domain of Human Guanylate Binding Protein 1 (HGBP1) in Complex with Non-Hydrolysable Gtp Analogue Gppnhp (pdb code 2bc9). 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 Crystal-Structure of the N-Terminal Large Gtpase Domain of Human Guanylate Binding Protein 1 (HGBP1) in Complex with Non-Hydrolysable Gtp Analogue Gppnhp, PDB code: 2bc9:

Magnesium binding site 1 out of 1 in the Crystal-Structure of the N-Terminal Large Gtpase Domain of Human Guanylate Binding Protein 1 (HGBP1) in Complex with Non-Hydrolysable Gtp Analogue Gppnhp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal-Structure of the N-Terminal Large Gtpase Domain of Human Guanylate Binding Protein 1 (HGBP1) in Complex with Non-Hydrolysable Gtp Analogue Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg595 b:38.2 occ:1.00 OG A:SER52 2.1 43.5 1.0 O2G A:GNP593 2.1 40.7 1.0 O2B A:GNP593 2.2 46.5 1.0 OG1 A:THR75 2.3 55.2 1.0 O A:HOH632 2.3 44.3 1.0 O A:HOH631 2.4 46.8 1.0 CB A:THR75 2.9 52.1 1.0 CB A:SER52 3.4 46.0 1.0 PB A:GNP593 3.4 46.2 1.0 PG A:GNP593 3.4 46.1 1.0 N3B A:GNP593 3.7 44.7 1.0 OD2 A:ASP97 3.8 50.8 1.0 N A:THR75 3.8 52.1 1.0 CA A:THR75 3.9 52.3 1.0 O2A A:GNP593 4.0 49.5 1.0 CG2 A:THR75 4.0 50.2 1.0 OD1 A:ASP97 4.0 50.8 1.0 O3G A:GNP593 4.1 44.6 1.0 O A:SER66 4.1 52.0 1.0 N A:SER52 4.1 44.1 1.0 CG A:ASP97 4.3 48.7 1.0 CA A:SER52 4.3 46.1 1.0 O1B A:GNP593 4.4 45.2 1.0 O3A A:GNP593 4.5 47.2 1.0 O1G A:GNP593 4.6 44.6 1.0 O A:THR98 4.6 39.2 1.0 PA A:GNP593 4.6 47.1 1.0 ND1 A:HIS74 4.7 51.1 1.0 O1A A:GNP593 4.9 45.8 1.0 C A:HIS74 5.0 53.5 1.0

A.Ghosh, G.J.Praefcke, L.Renault, A.Wittinghofer, C.Herrmann. How Guanylate-Binding Proteins Achieve Assembly-Stimulated Processive Cleavage of Gtp to Gmp. Nature V. 440 101 2006.
ISSN: ISSN 0028-0836
PubMed: 16511497
DOI: 10.1038/NATURE04510